NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|32445327|emb|CAD75328|]
View 

probable sepiapterin reductase homolog yueD [Rhodopirellula baltica SH 1]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143277)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase may catalyze isomerization, decarboxylation, epimerization, C=N bond reduction, dehydration, dehalogenation, enoyl-CoA reduction, and/or carbonyl-alcohol oxidoreduction; similar to sepiapterin reductase that catalyzes the final one or two reductions in tetra-hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 16-248 3.16e-75

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


:

Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 228.71  E-value: 3.16e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRGF--RVFAVGRSVELLQSLSEA--CGSRVTTVAADLCSIAGVEQLLASIPS-DSEIAG 90
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKRGSpsVVVLLARSEEPLQELKEElrPGLRVTTVKADLSDAAGVEQLLEAIRKlDGERDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  91 LVHSAGSLVPLQPYEQIDMNELAEHFRIHVGVPIELFNSLSRDC----TVKRMLFIDSYSASNARLGWGAYSIVKAAAQM 166
Cdd:cd05367  81 LINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFkkrgLKKTVVNVSSGAAVNPFKGWGLYCSSKAARDM 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327 167 AARCAAQELPGTRTIRAYPGAVNTRIVDAVLAS--DTQTASTFASMREKGEFAEPEDVARFLVALLVDATDEligSRDVF 244
Cdd:cd05367 161 FFRVLAAEEPDVRVLSYAPGVVDTDMQREIRETsaDPETRSRFRSLKEKGELLDPEQSAEKLANLLEKDKFE---SGAHV 237


                ....
gi 32445327 245 DYNN 248
Cdd:cd05367 238 DYYD 241
 
Name Accession Description Interval E-value
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 16-248 3.16e-75

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 228.71  E-value: 3.16e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRGF--RVFAVGRSVELLQSLSEA--CGSRVTTVAADLCSIAGVEQLLASIPS-DSEIAG 90
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKRGSpsVVVLLARSEEPLQELKEElrPGLRVTTVKADLSDAAGVEQLLEAIRKlDGERDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  91 LVHSAGSLVPLQPYEQIDMNELAEHFRIHVGVPIELFNSLSRDC----TVKRMLFIDSYSASNARLGWGAYSIVKAAAQM 166
Cdd:cd05367  81 LINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFkkrgLKKTVVNVSSGAAVNPFKGWGLYCSSKAARDM 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327 167 AARCAAQELPGTRTIRAYPGAVNTRIVDAVLAS--DTQTASTFASMREKGEFAEPEDVARFLVALLVDATDEligSRDVF 244
Cdd:cd05367 161 FFRVLAAEEPDVRVLSYAPGVVDTDMQREIRETsaDPETRSRFRSLKEKGELLDPEQSAEKLANLLEKDKFE---SGAHV 237


                ....
gi 32445327 245 DYNN 248
Cdd:cd05367 238 DYYD 241
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
15-230 1.60e-26

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 103.41  E-value: 1.60e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  15 PTYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEAC---GSRVTTVAADLCSIAGVEQLLASIPSDS-EIAG 90
Cdd:COG0300   6 KTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELraaGARVEVVALDVTDPDAVAALAEAVLARFgPIDV 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  91 LVHSAGSLVPlQPYEQIDMNELAEHFRIHVGVPIELFNSLsrdctVKRM--------LFIDSYSASNARLGWGAYSIVKA 162
Cdd:COG0300  86 LVNNAGVGGG-GPFEELDLEDLRRVFEVNVFGPVRLTRAL-----LPLMrargrgriVNVSSVAGLRGLPGMAAYAASKA 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32445327 163 AAQMAARCAAQELPGTRtIRA---YPGAVNTRIVDAvlasdtqtastfASMREKGEFAEPEDVARFLVALL 230
Cdd:COG0300 160 ALEGFSESLRAELAPTG-VRVtavCPGPVDTPFTAR------------AGAPAGRPLLSPEEVARAILRAL 217
PRK07023 PRK07023
SDR family oxidoreductase;
17-232 7.99e-25

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 98.93  E-value: 7.99e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   17 YVVTGATRGIGRAVAKELAGRGFRVFAVGRSVEllQSLSEACGSRVTTVAADLCSIAGVEQLLAS-----IPSDSEIAGL 91
Cdd:PRK07023   4 AIVTGHSRGLGAALAEQLLQPGIAVLGVARSRH--PSLAAAAGERLAEVELDLSDAAAAAAWLAGdllaaFVDGASRVLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   92 VHSAGSLVPLQPYEQIDMNELAEHFRIHVGVPIELFNSLSR---DCTVKRMLFIDSYSASNARLGWGAYSIVKAAAQMAA 168
Cdd:PRK07023  82 INNAGTVEPIGPLATLDAAAIARAVGLNVAAPLMLTAALAQaasDAAERRILHISSGAARNAYAGWSVYCATKAALDHHA 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  169 RCAAQElpGTRTIRA---YPGAVNTRIVDAVLASDTQT---ASTFASMREKGEFAEPEDVARFLVALLVD 232
Cdd:PRK07023 162 RAVALD--ANRALRIvslAPGVVDTGMQATIRATDEERfpmRERFRELKASGALSTPEDAARRLIAYLLS 229
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 18-111 1.69e-13

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 67.25  E-value: 1.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327    18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSE---ACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLVH 93
Cdd:pfam00106   4 LVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKelgALGGKALFIQGDVTDRAQVKALVEQAVERlGRLDILVN 83

                          90
                  ....*....|....*...
gi 32445327    94 SAGsLVPLQPYEQIDMNE 111
Cdd:pfam00106  84 NAG-ITGLGPFSELSDED 100
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 16-117 7.52e-13

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 65.20  E-value: 7.52e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327     16 TYVVTGATRGIGRAVAKELAGRGFRVFA-VGRS-------VELLQSLSEAcGSRVTTVAADLCSIAGVEQLLASIPSDS- 86
Cdd:smart00822   2 TYLITGGLGGLGRALARWLAERGARRLVlLSRSgpdapgaAALLAELEAA-GARVTVVACDVADRDALAAVLAAIPAVEg 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 32445327     87 EIAGLVHSAGSLvPLQPYEQIDMNELAEHFR 117
Cdd:smart00822  81 PLTGVIHAAGVL-DDGVLASLTPERFAAVLA 110
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 18-230 2.07e-11

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 62.24  E-value: 2.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327    18 VVTGATRGIGRAVAKELAGR----GFRVFAVGRSVELLQSLSEACGS-----RVTTVAADLCSIAGVEQLLASI-----P 83
Cdd:TIGR01500   4 LVTGASRGFGRTIAQELAKClkspGSVLVLSARNDEALRQLKAEIGAersglRVVRVSLDLGAEAGLEQLLKALrelprP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327    84 SDSEIAGLVHSAGSLVPLQPYEQidmnELAEHFRIHVGVPIELFNSLSRDCTVKRML-----------FIDSYSASNARL 152
Cdd:TIGR01500  84 KGLQRLLLINNAGTLGDVSKGFV----DLSDSTQVQNYWALNLTSMLCLTSSVLKAFkdspglnrtvvNISSLCAIQPFK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   153 GWGAYSIVKAAAQMAARCAAQE--LPGTRTIRAYPGAVNTRIVDAVL--ASDTQTASTFASMREKGEFAEPEDVARFLVA 228
Cdd:TIGR01500 160 GWALYCAGKAARDMLFQVLALEekNPNVRVLNYAPGVLDTDMQQQVReeSVDPDMRKGLQELKAKGKLVDPKVSAQKLLS 239


                  ..
gi 32445327   229 LL 230
Cdd:TIGR01500 240 LL 241
 
Name Accession Description Interval E-value
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 16-248 3.16e-75

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 228.71  E-value: 3.16e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRGF--RVFAVGRSVELLQSLSEA--CGSRVTTVAADLCSIAGVEQLLASIPS-DSEIAG 90
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKRGSpsVVVLLARSEEPLQELKEElrPGLRVTTVKADLSDAAGVEQLLEAIRKlDGERDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  91 LVHSAGSLVPLQPYEQIDMNELAEHFRIHVGVPIELFNSLSRDC----TVKRMLFIDSYSASNARLGWGAYSIVKAAAQM 166
Cdd:cd05367  81 LINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFkkrgLKKTVVNVSSGAAVNPFKGWGLYCSSKAARDM 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327 167 AARCAAQELPGTRTIRAYPGAVNTRIVDAVLAS--DTQTASTFASMREKGEFAEPEDVARFLVALLVDATDEligSRDVF 244
Cdd:cd05367 161 FFRVLAAEEPDVRVLSYAPGVVDTDMQREIRETsaDPETRSRFRSLKEKGELLDPEQSAEKLANLLEKDKFE---SGAHV 237


                ....
gi 32445327 245 DYNN 248
Cdd:cd05367 238 DYYD 241
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 18-240 1.09e-26

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 103.52  E-value: 1.09e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSL--SEACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLVHS 94
Cdd:cd05233   2 LVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELaaIEALGGNAVAVQADVSDEEDVEALVEEALEEfGRLDILVNN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  95 AGSLVPlQPYEQIDMNELAEHFRIHVGVPIelfnSLSRDCtVKRML--------FIDSYSASNARLGWGAYSIVKAAAQM 166
Cdd:cd05233  82 AGIARP-GPLEELTDEDWDRVLDVNLTGVF----LLTRAA-LPHMKkqgggrivNISSVAGLRPLPGQAAYAASKAALEG 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32445327 167 AARCAAQELPGTRtIRA---YPGAVNTRIVDAVlaSDTQTASTFASMREKGEFAEPEDVARFLVALLVDATDELIGS 240
Cdd:cd05233 156 LTRSLALELAPYG-IRVnavAPGLVDTPMLAKL--GPEEAEKELAAAIPLGRLGTPEEVAEAVVFLASDEASYITGQ 229
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
15-230 1.60e-26

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 103.41  E-value: 1.60e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  15 PTYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEAC---GSRVTTVAADLCSIAGVEQLLASIPSDS-EIAG 90
Cdd:COG0300   6 KTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELraaGARVEVVALDVTDPDAVAALAEAVLARFgPIDV 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  91 LVHSAGSLVPlQPYEQIDMNELAEHFRIHVGVPIELFNSLsrdctVKRM--------LFIDSYSASNARLGWGAYSIVKA 162
Cdd:COG0300  86 LVNNAGVGGG-GPFEELDLEDLRRVFEVNVFGPVRLTRAL-----LPLMrargrgriVNVSSVAGLRGLPGMAAYAASKA 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32445327 163 AAQMAARCAAQELPGTRtIRA---YPGAVNTRIVDAvlasdtqtastfASMREKGEFAEPEDVARFLVALL 230
Cdd:COG0300 160 ALEGFSESLRAELAPTG-VRVtavCPGPVDTPFTAR------------AGAPAGRPLLSPEEVARAILRAL 217
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 15-230 7.25e-26

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 101.41  E-value: 7.25e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  15 PTYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLVH 93
Cdd:COG4221   6 KVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEfGRLDVLVN 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  94 SAGsLVPLQPYEQIDMNELAEHFRIHV-GVpielFNslsrdCT---VKRM--------LFIDSYSASNARLGWGAYSIVK 161
Cdd:COG4221  86 NAG-VALLGPLEELDPEDWDRMIDVNVkGV----LY-----VTraaLPAMrargsghiVNISSIAGLRPYPGGAVYAATK 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32445327 162 AAAQMAARCAAQELPGTRtIRA---YPGAVNTRIVDAVLASDTQTAstfASMREKGEFAEPEDVARFLVALL 230
Cdd:COG4221 156 AAVRGLSESLRAELRPTG-IRVtviEPGAVDTEFLDSVFDGDAEAA---AAVYEGLEPLTPEDVAEAVLFAL 223
PRK07023 PRK07023
SDR family oxidoreductase;
17-232 7.99e-25

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 98.93  E-value: 7.99e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   17 YVVTGATRGIGRAVAKELAGRGFRVFAVGRSVEllQSLSEACGSRVTTVAADLCSIAGVEQLLAS-----IPSDSEIAGL 91
Cdd:PRK07023   4 AIVTGHSRGLGAALAEQLLQPGIAVLGVARSRH--PSLAAAAGERLAEVELDLSDAAAAAAWLAGdllaaFVDGASRVLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   92 VHSAGSLVPLQPYEQIDMNELAEHFRIHVGVPIELFNSLSR---DCTVKRMLFIDSYSASNARLGWGAYSIVKAAAQMAA 168
Cdd:PRK07023  82 INNAGTVEPIGPLATLDAAAIARAVGLNVAAPLMLTAALAQaasDAAERRILHISSGAARNAYAGWSVYCATKAALDHHA 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  169 RCAAQElpGTRTIRA---YPGAVNTRIVDAVLASDTQT---ASTFASMREKGEFAEPEDVARFLVALLVD 232
Cdd:PRK07023 162 RAVALD--ANRALRIvslAPGVVDTGMQATIRATDEERfpmRERFRELKASGALSTPEDAARRLIAYLLS 229
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 18-233 8.47e-24

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 96.01  E-value: 8.47e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSE---ACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLVH 93
Cdd:COG1028  10 LVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAelrAAGGRALAVAADVTDEAAVEALVAAAVAAfGRLDILVN 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  94 SAGSLVPlQPYEQIDMNELAEHFRIHV-GVpielFNsLSRDCtVKRM--------LFIDSYSASNARLGWGAYSIVKAAA 164
Cdd:COG1028  90 NAGITPP-GPLEELTEEDWDRVLDVNLkGP----FL-LTRAA-LPHMrergggriVNISSIAGLRGSPGQAAYAASKAAV 162

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32445327 165 QMAARCAAQELpGTRTIRAY---PGAVNTRIVDAVLASDTQTAStFASMREKGEFAEPEDVARFLVALLVDA 233
Cdd:COG1028 163 VGLTRSLALEL-APRGIRVNavaPGPIDTPMTRALLGAEEVREA-LAARIPLGRLGTPEEVAAAVLFLASDA 232
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
17-232 1.13e-22

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 93.21  E-value: 1.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   17 YVVTGATRGIGRAVAKELAGRGFRVFAVGRS-VELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSDSEIAG----- 90
Cdd:PRK06924   4 VIITGTSQGLGEAIANQLLEKGTHVISISRTeNKELTKLAEQYNSNLTFHSLDLQDVHELETNFNEILSSIQEDNvssih 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   91 LVHSAGSLVPLQPYEQIDMNELAEHFRIHVGVPIELFNSL-----SRDCTvKRMLFIDSYSASNARLGWGAYSIVKA--- 162
Cdd:PRK06924  84 LINNAGMVAPIKPIEKAESEELITNVHLNLLAPMILTSTFmkhtkDWKVD-KRVINISSGAAKNPYFGWSAYCSSKAgld 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32445327  163 --AAQMAARCAAQELPgTRTIRAYPGAVNTRIVDAVLAS---DTQTASTFASMREKGEFAEPEDVARFLVALLVD 232
Cdd:PRK06924 163 mfTQTVATEQEEEEYP-VKIVAFSPGVMDTNMQAQIRSSskeDFTNLDRFITLKEEGKLLSPEYVAKALRNLLET 236
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 15-244 1.92e-20

HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 86.65  E-value: 1.92e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  15 PTYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSeACGSRVTTVAADLCSIAGVEQLLASIPSDSE-IAGLVH 93
Cdd:cd08932   1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALS-ASGGDVEAVPYDARDPEDARALVDALRDRFGrIDVLVH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  94 SAGSLVPLqPYEQIDMNELAEHFRIHVGVPIEL----FNSLsRDCTVKRMLFIDSYSASNARLGWGAYSIVKAAAQMAAR 169
Cdd:cd08932  80 NAGIGRPT-TLREGSDAELEAHFSINVIAPAELtralLPAL-REAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRALAH 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32445327 170 CAAQELPGTrTIRAY---PGAVNTRIVdavlasdtqTASTFASMREKGEFAEPEDVARfLVALLVDATdELIGSRDVF 244
Cdd:cd08932 158 ALRQEGWDH-GVRVSavcPGFVDTPMA---------QGLTLVGAFPPEEMIQPKDIAN-LVRMVIELP-ENITSVAVL 223
PRK07454 PRK07454
SDR family oxidoreductase;
9-195 6.37e-18

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 80.39  E-value: 6.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327    9 SNMQAIPTYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEAC---GSRVTTVAADLCSIAGVEQLLASIPSD 85
Cdd:PRK07454   1 MSLNSMPRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELrstGVKAAAYSIDLSNPEAIAPGIAELLEQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   86 SE-IAGLVHSAG-----SLV--PLQPYEQ-IDMNeLAEHFRIHVGVpielfnslsrdctVKRM------LFID--SYSAS 148
Cdd:PRK07454  81 FGcPDVLINNAGmaytgPLLemPLSDWQWvIQLN-LTSVFQCCSAV-------------LPGMrargggLIINvsSIAAR 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 32445327  149 NARLGWGAYSIVKAAAQMAARCAAQE--LPGTRTIRAYPGAVNTRIVDA 195
Cdd:PRK07454 147 NAFPQWGAYCVSKAALAAFTKCLAEEerSHGIRVCTITLGAVNTPLWDT 195
PRK08219 PRK08219
SDR family oxidoreductase;
15-236 7.19e-17

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 76.90  E-value: 7.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   15 PTYVVTGATRGIGRAVAKELAgRGFRVFAVGRSVELLQSLSEACGSrVTTVAADLCSIAGVEQLLASIPsdsEIAGLVHS 94
Cdd:PRK08219   4 PTALITGASRGIGAAIARELA-PTHTLLLGGRPAERLDELAAELPG-ATPFPVDLTDPEAIAAAVEQLG---RLDVLVHN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   95 AGsLVPLQPYEQIDMNELAEHFRIHVGVPIELFNSL------SRDCTVkrmlFIDSYSASNARLGWGAYSIVKAAAQMAA 168
Cdd:PRK08219  79 AG-VADLGPVAESTVDEWRATLEVNVVAPAELTRLLlpalraAHGHVV----FINSGAGLRANPGWGSYAASKFALRALA 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32445327  169 RCAAQELPGT-RTIRAYPGAVNTRIVDAVLAsdtQTASTFasmrEKGEFAEPEDVARfLVALLVDATDE 236
Cdd:PRK08219 154 DALREEEPGNvRVTSVHPGRTDTDMQRGLVA---QEGGEY----DPERYLRPETVAK-AVRFAVDAPPD 214
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 18-240 9.69e-17

xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins identified as L-xylulose reductase (XR) and carbonyl reductase; they are members of the SDR family. XR, catalyzes the NADP-dependent reduction of L-xyulose and other sugars. Tetrameric mouse carbonyl reductase is involved in the metabolism of biogenic and xenobiotic carbonyl compounds. This subgroup also includes tetrameric chicken liver D-erythrulose reductase, which catalyzes the reduction of D-erythrulose to D-threitol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 77.13  E-value: 9.69e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSrVTTVAADLCSIAGVEQLLASIPSdseIAGLVHSAGs 97
Cdd:cd05351  11 LVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVRECPG-IEPVCVDLSDWDATEEALGSVGP---VDLLVNNAA- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  98 LVPLQPYEQIDMNELAEHFRIHVGVPIELFNSLSRDCTVKR----MLFIDSYSASNARLGWGAYSIVKAAAQMAARCAAQ 173
Cdd:cd05351  86 VAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvpgsIVNVSSQASQRALTNHTVYCSTKAALDMLTKVMAL 165

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32445327 174 ELpGTRTIRAypGAVNTRIV----DAVLASDTQTASTFASMREKGEFAEPEDVARFLVALLVDATDELIGS 240
Cdd:cd05351 166 EL-GPHKIRV--NSVNPTVVmtdmGRDNWSDPEKAKKMLNRIPLGKFAEVEDVVNAILFLLSDKSSMTTGS 233
PRK09072 PRK09072
SDR family oxidoreductase;
18-126 7.69e-16

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 74.98  E-value: 7.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEAC--GSRVTTVAADLCSIAGVEQLLASIPSDSEIAGLVHSA 95
Cdd:PRK09072   9 LLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLpyPGRHRWVVADLTSEAGREAVLARAREMGGINVLINNA 88

                         90       100       110
                 ....*....|....*....|....*....|...
gi 32445327   96 G--SLVPLqpyEQIDMNELAEHFRIHVGVPIEL 126
Cdd:PRK09072  89 GvnHFALL---EDQDPEAIERLLALNLTAPMQL 118
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 16-237 1.34e-15

17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 73.80  E-value: 1.34e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIpsdSEIAG----L 91
Cdd:cd05374   2 VVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVLELDVTDEESIKAAVKEV---IERFGridvL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  92 VHSAGSLVpLQPYEQIDMNELAEHFRIHVGVPIELfnslsrdctVK------------RMLFIDSYSASNARLGWGAYSI 159
Cdd:cd05374  79 VNNAGYGL-FGPLEETSIEEVRELFEVNVFGPLRV---------TRaflplmrkqgsgRIVNVSSVAGLVPTPFLGPYCA 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327 160 VKAAAQMAARCAAQEL--PGTRTIRAYPGAVNTRIVDAVLASDTQ--TASTFASMREK---------GEFAEPEDVARFL 226
Cdd:cd05374 149 SKAALEALSESLRLELapFGIKVTIIEPGPVRTGFADNAAGSALEdpEISPYAPERKEikenaagvgSNPGDPEKVADVI 228

                       250
                ....*....|.
gi 32445327 227 VALLVDATDEL 237
Cdd:cd05374 229 VKALTSESPPL 239
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 18-239 3.13e-15

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 72.67  E-value: 3.13e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEAC-------GSRVTTVAADLCSIAGVEQLLA-SIPSDSEIA 89
Cdd:cd08939   5 LITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIeaeanasGQKVSYISADLSDYEEVEQAFAqAVEKGGPPD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  90 GLVHSAGSLVPL----QPYEQ----IDMNELAEHFRIHVGVPIELFNSlsrdctVKRMLFIDSYSASNARLGWGAYSIVK 161
Cdd:cd08939  85 LVVNCAGISIPGlfedLTAEEfergMDVNYFGSLNVAHAVLPLMKEQR------PGHIVFVSSQAALVGIYGYSAYCPSK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327 162 AAAQMAARCAAQEL--PGTRTIRAYPGAVNTRIVDAVLAsdTQTASTfASMREKGEFAEPEDVARFLVALL----VDATD 235
Cdd:cd08939 159 FALRGLAESLRQELkpYNIRVSVVYPPDTDTPGFEEENK--TKPEET-KAIEGSSGPITPEEAARIIVKGLdrgyDDVFT 235


                ....
gi 32445327 236 ELIG 239
Cdd:cd08939 236 DFIG 239
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
18-96 1.94e-14

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 70.57  E-value: 1.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSE---ACGSRVTTVAADLCSIAGVEQLLASIP-SDSEIAGLVH 93
Cdd:PRK05653   9 LVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAelrAAGGEARVLVFDVSDEAAVRALIEAAVeAFGALDILVN 88


                 ...
gi 32445327   94 SAG 96
Cdd:PRK05653  89 NAG 91
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 16-230 3.51e-14

tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup includes TR-I and TR-II; these proteins are members of the SDR family. TRs catalyze the NADPH-dependent reductions of the 3-carbonyl group of tropinone, to a beta-hydroxyl group. TR-I and TR-II produce different stereoisomers from tropinone, TR-I produces tropine (3alpha-hydroxytropane), and TR-II, produces pseudotropine (sigma-tropine, 3beta-hydroxytropane). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187590 [Multi-domain]  Cd Length: 251  Bit Score: 70.17  E-value: 3.51e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSR---VTTVAADLCSIAGVEQLLASIPS--DSEIAG 90
Cdd:cd05329   8 TALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKgfkVEGSVCDVSSRSERQELMDTVAShfGGKLNI 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  91 LVHSAGSLVplqPYEQIDMNElaEHFRIHVGVPIE-------LFNSLSRDCTVKRMLFIDSYSASNARLGWGAYSIVKAA 163
Cdd:cd05329  88 LVNNAGTNI---RKEAKDYTE--EDYSLIMSTNFEaayhlsrLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATKGA 162

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32445327 164 AQMAARCAAQELP--GTRTIRAYPGAVNTRIVDAVLaSDTQTASTFASMREKGEFAEPEDVARfLVALL 230
Cdd:cd05329 163 LNQLTRSLACEWAkdNIRVNAVAPWVIATPLVEPVI-QQKENLDKVIERTPLKRFGEPEEVAA-LVAFL 229
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 16-98 5.84e-14

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 70.49  E-value: 5.84e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRGFRVFA-VGRS-----VELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSDSEIA 89
Cdd:cd05274 152 TYLITGGLGGLGLLVARWLAARGARHLVlLSRRgpaprAAARAALLRAGGARVSVVRCDVTDPAALAALLAELAAGGPLA 231


                ....*....
gi 32445327  90 GLVHSAGSL 98
Cdd:cd05274 232 GVIHAAGVL 240
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 15-135 7.86e-14

pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR family, catalyzes the NAD-dependent reduction of folic acid, dihydrofolate and related compounds. In Leishmania, pteridine reductase (PTR1) acts to circumvent the anti-protozoan drugs that attack dihydrofolate reductase activity. Proteins in this subgroup have an N-terminal NAD-binding motif and a YxxxK active site motif, but have an Asp instead of the usual upstream catalytic Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 68.84  E-value: 7.86e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  15 PTYVVTGATRGIGRAVAKELAGRGFRVFA-VGRSVELLQSLS---EACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIA 89
Cdd:cd05357   1 AVALVTGAAKRIGRAIAEALAAEGYRVVVhYNRSEAEAQRLKdelNALRNSAVLVQADLSDFAACADLVAAAFRAfGRCD 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32445327  90 GLVHSAGSLVPlQPYEQIDMNELAEHFRIHVGVPIELFNSLSRDCT 135
Cdd:cd05357  81 VLVNNASAFYP-TPLGQGSEDAWAELFGINLKAPYLLIQAFARRLA 125
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 18-111 1.69e-13

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 67.25  E-value: 1.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327    18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSE---ACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLVH 93
Cdd:pfam00106   4 LVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKelgALGGKALFIQGDVTDRAQVKALVEQAVERlGRLDILVN 83

                          90
                  ....*....|....*...
gi 32445327    94 SAGsLVPLQPYEQIDMNE 111
Cdd:pfam00106  84 NAG-ITGLGPFSELSDED 100
PRK06484 PRK06484
short chain dehydrogenase; Validated
 16-255 2.55e-13

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 69.11  E-value: 2.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLVHS 94
Cdd:PRK06484 271 VVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQARwGRLDVLVNN 350

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   95 AGSLVPLQPYEQIDMNELAEHFRIHVGVPI----ELFNSLSRDCTVKRMLFIDSYSASNARLGWGAYsivKAAAQMAARC 170
Cdd:PRK06484 351 AGIAEVFKPSLEQSAEDFTRVYDVNLSGAFacarAAARLMSQGGVIVNLGSIASLLALPPRNAYCAS---KAAVTMLSRS 427

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  171 AAQELP--GTRTIRAYPGAVNTRIVDAVLASdtqTASTFASMREK---GEFAEPEDVARFLVALLVDATDELIGSRDVFD 245
Cdd:PRK06484 428 LACEWApaGIRVNTVAPGYIETPAVLALKAS---GRADFDSIRRRiplGRLGDPEEVAEAIAFLASPAASYVNGATLTVD 504

                        250
                 ....*....|....*
gi 32445327  246 -----YNNPGDRADV 255
Cdd:PRK06484 505 ggwtaFGDAGDASDP 519
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 16-100 4.43e-13

retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs; Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 67.25  E-value: 4.43e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQS-----LSEACGSRVTTVAADLCSIAGV----EQLLASIPsds 86
Cdd:cd05327   3 VVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEaaaeiKKETGNAKVEVIQLDLSSLASVrqfaEEFLARFP--- 79

                        90
                ....*....|....
gi 32445327  87 EIAGLVHSAGSLVP 100
Cdd:cd05327  80 RLDILINNAGIMAP 93
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 16-117 7.52e-13

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 65.20  E-value: 7.52e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327     16 TYVVTGATRGIGRAVAKELAGRGFRVFA-VGRS-------VELLQSLSEAcGSRVTTVAADLCSIAGVEQLLASIPSDS- 86
Cdd:smart00822   2 TYLITGGLGGLGRALARWLAERGARRLVlLSRSgpdapgaAALLAELEAA-GARVTVVACDVADRDALAAVLAAIPAVEg 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 32445327     87 EIAGLVHSAGSLvPLQPYEQIDMNELAEHFR 117
Cdd:smart00822  81 PLTGVIHAAGVL-DDGVLASLTPERFAAVLA 110
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 19-233 1.08e-12

2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 dihydrozybenzoate dehydrogenase shares the characteristics of the classical SDRs. This subgroup includes Escherichai coli EntA which catalyzes the NAD+-dependent oxidation of 2,3-dihydro-2,3-dihydroxybenzoate to 2,3-dihydroxybenzoate during biosynthesis of the siderophore Enterobactin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 65.95  E-value: 1.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  19 VTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQslseACGSRVTTVAADLCSIAGVEQLLASIPSDSE-IAGLVHSAGS 97
Cdd:cd05331   3 VTGAAQGIGRAVARHLLQAGATVIALDLPFVLLL----EYGDPLRLTPLDVADAAAVREVCSRLLAEHGpIDALVNCAGV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  98 LVPlQPYEQIDMNELAEHFRIHVGVPIELFNSLSRDCTVKR---MLFIDSYSASNARLGWGAYSIVKAAAQMAARCAAQE 174
Cdd:cd05331  79 LRP-GATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRtgaIVTVASNAAHVPRISMAAYGASKAALASLSKCLGLE 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32445327 175 LP--GTRTIRAYPGAVNTRIVDAVLASDTQTASTFASMREK-------GEFAEPEDVARFLVALLVDA 233
Cdd:cd05331 158 LApyGVRCNVVSPGSTDTAMQRTLWHDEDGAAQVIAGVPEQfrlgiplGKIAQPADIANAVLFLASDQ 225
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 18-224 2.28e-12

clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent reduction of clavulanate-9-aldehyde to clavulanic acid, a beta-lactamase inhibitor. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187639 [Multi-domain]  Cd Length: 243  Bit Score: 64.87  E-value: 2.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLS---EACGSRVTTVAADLCSIAGVEQLLASipSDSEIAG---L 91
Cdd:cd08934   7 LVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALAdelEAEGGKALVLELDVTDEQQVDAAVER--TVEALGRldiL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  92 VHSAGSLVpLQPYE---------QIDMNELAEHFRIHVGVPIELFNSlsrdctVKRMLFIDSYSASNARLGWGAYSIVKA 162
Cdd:cd08934  85 VNNAGIML-LGPVEdadttdwtrMIDTNLLGLMYTTHAALPHHLLRN------KGTIVNISSVAGRVAVRNSAVYNATKF 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32445327 163 AAQMAARCAAQE--LPGTRTIRAYPGAVNTRIVDAVLASDTQTAST--FASMREkgefAEPEDVAR 224
Cdd:cd08934 158 GVNAFSEGLRQEvtERGVRVVVIEPGTVDTELRDHITHTITKEAYEerISTIRK----LQAEDIAA 219
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 16-98 2.38e-12

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 66.24  E-value: 2.38e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  16 TYVVTGATRGIGRAVAKELAGR-GFRVFAVGRS---------VELLQSLSEAcGSRVTTVAADLCSIAGVEQLLASIPSD 85
Cdd:cd08953 207 VYLVTGGAGGIGRALARALARRyGARLVLLGRSplppeeewkAQTLAALEAL-GARVLYISADVTDAAAVRRLLEKVRER 285

                        90
                ....*....|....
gi 32445327  86 S-EIAGLVHSAGSL 98
Cdd:cd08953 286 YgAIDGVIHAAGVL 299
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 17-161 2.56e-12

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 64.62  E-value: 2.56e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  17 YVVTGATRGIGRAVAKELAGRG-FRVFAVGRSVELLQSLS--EACGSRVTTVAADLCSIAgvEQLLASIPSDSEIAGL-- 91
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGnNTVIATCRDPSAATELAalGASHSRLHILELDVTDEI--AESAEAVAERLGDAGLdv 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32445327  92 -VHSAGSLVPLQPYEQIDMNELAEHFRIHVGVPIELFNS---LSRDCTVKRMLFIDSYSAS---NARLGWGAYSIVK 161
Cdd:cd05325  79 lINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAflpLLLKGARAKIINISSRVGSigdNTSGGWYSYRASK 155
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 15-111 3.70e-12

classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 64.22  E-value: 3.70e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  15 PTYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGS----RVTTVAADLCSIAGVEQLLASIPSD-SEIA 89
Cdd:cd05346   1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAkfpvKVLPLQLDVSDRESIEAALENLPEEfRDID 80

                        90       100
                ....*....|....*....|..
gi 32445327  90 GLVHSAGSLVPLQPYEQIDMNE 111
Cdd:cd05346  81 ILVNNAGLALGLDPAQEADLED 102
PRK12826 PRK12826
SDR family oxidoreductase;
18-231 6.65e-12

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 63.78  E-value: 6.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEAC---GSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLVH 93
Cdd:PRK12826  10 LVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVeaaGGKARARQVDVRDRAALKAAVAAGVEDfGRLDILVA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   94 SAGsLVPLQPYEQ---------IDMNELAEHFRIHVGVPielfnsLSRDCTVKRMLFIDSYSASN-ARLGWGAYSIVKAA 163
Cdd:PRK12826  90 NAG-IFPLTPFAEmddeqwervIDVNLTGTFLLTQAALP------ALIRAGGGRIVLTSSVAGPRvGYPGLAHYAASKAG 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32445327  164 AQMAARCAAQELpGTRTIR---AYPGAVNT-RIVDAVLASDTQTASTFASMrekGEFAEPEDVARfLVALLV 231
Cdd:PRK12826 163 LVGFTRALALEL-AARNITvnsVHPGGVDTpMAGNLGDAQWAEAIAAAIPL---GRLGEPEDIAA-AVLFLA 229
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 16-98 8.88e-12

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 62.19  E-value: 8.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327    16 TYVVTGATRGIGRAVAKELAGRGFR-VFAVGRS-------VELLQSLsEACGSRVTTVAADLCSIAGVEQLLASIPSD-S 86
Cdd:pfam08659   2 TYLITGGLGGLGRELARWLAERGARhLVLLSRSaaprpdaQALIAEL-EARGVEVVVVACDVSDPDAVAALLAEIKAEgP 80

                          90
                  ....*....|..
gi 32445327    87 EIAGLVHSAGSL 98
Cdd:pfam08659  81 PIRGVIHAAGVL 92
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 15-232 1.90e-11

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) SDR; This subgroup includes Escherichia coli CFT073 FabG. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187596 [Multi-domain]  Cd Length: 255  Bit Score: 62.48  E-value: 1.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  15 PTYVVTGATRGIGRAVAKELAGRGFRVFAVGR----SVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIA 89
Cdd:cd05337   2 PVAIVTGASRGIGRAIATELAARGFDIAINDLpdddQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDfGRLD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  90 GLVHSAGslvpLQPYEQIDMNELAEH-----FRIHVGVPIELFNSLSR---------DCTVKRMLFIDSYSASNARLGWG 155
Cdd:cd05337  82 CLVNNAG----IAVRPRGDLLDLTEDsfdrlIAINLRGPFFLTQAVARrmveqpdrfDGPHRSIIFVTSINAYLVSPNRG 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327 156 AYSIVKAAAQMAARCAAQELpGTRTIRAY---PGAVNT-RIVDAVLASDTQTASTFASMREKGefaEPEDVARFLVALLV 231
Cdd:cd05337 158 EYCISKAGLSMATRLLAYRL-ADEGIAVHeirPGLIHTdMTAPVKEKYDELIAAGLVPIRRWG---QPEDIAKAVRTLAS 233


                .
gi 32445327 232 D 232
Cdd:cd05337 234 G 234
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 18-230 2.07e-11

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 62.24  E-value: 2.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327    18 VVTGATRGIGRAVAKELAGR----GFRVFAVGRSVELLQSLSEACGS-----RVTTVAADLCSIAGVEQLLASI-----P 83
Cdd:TIGR01500   4 LVTGASRGFGRTIAQELAKClkspGSVLVLSARNDEALRQLKAEIGAersglRVVRVSLDLGAEAGLEQLLKALrelprP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327    84 SDSEIAGLVHSAGSLVPLQPYEQidmnELAEHFRIHVGVPIELFNSLSRDCTVKRML-----------FIDSYSASNARL 152
Cdd:TIGR01500  84 KGLQRLLLINNAGTLGDVSKGFV----DLSDSTQVQNYWALNLTSMLCLTSSVLKAFkdspglnrtvvNISSLCAIQPFK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   153 GWGAYSIVKAAAQMAARCAAQE--LPGTRTIRAYPGAVNTRIVDAVL--ASDTQTASTFASMREKGEFAEPEDVARFLVA 228
Cdd:TIGR01500 160 GWALYCAGKAARDMLFQVLALEekNPNVRVLNYAPGVLDTDMQQQVReeSVDPDMRKGLQELKAKGKLVDPKVSAQKLLS 239


                  ..
gi 32445327   229 LL 230
Cdd:TIGR01500 240 LL 241
PRK08703 PRK08703
SDR family oxidoreductase;
16-190 2.12e-11

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 62.26  E-value: 2.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQ----SLSEACGSRVTTVAADLCSIAG--VEQLLASIPSDSE-- 87
Cdd:PRK08703   8 TILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEkvydAIVEAGHPEPFAIRFDLMSAEEkeFEQFAATIAEATQgk 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   88 IAGLVHSAGSLVPLQPYEQIDMNELAEHFRIHVGVPIELFNSL------SRDCTVkrmLFIDSYSASNARLGWGAYSIVK 161
Cdd:PRK08703  88 LDGIVHCAGYFYALSPLDFQTVAEWVNQYRINTVAPMGLTRALfpllkqSPDASV---IFVGESHGETPKAYWGGFGASK 164

                        170       180       190
                 ....*....|....*....|....*....|..
gi 32445327  162 AAAQMAARCAAQE---LPGTRTIRAYPGAVNT 190
Cdd:PRK08703 165 AALNYLCKVAADEwerFGNLRANVLVPGPINS 196
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 18-96 2.31e-11

17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) SDRs; This subgroup includes various 17-beta-hydroxysteroid dehydrogenases and 3-ketoacyl-CoA reductase, these are members of the SDR family, and contain the canonical active site tetrad and glycine-rich NAD-binding motif of the classical SDRs. 3-ketoacyl-CoA reductase (KAR, aka 17beta-HSD type 12, encoded by HSD17B12) acts in fatty acid elongation; 17beta- hydroxysteroid dehydrogenases are isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 17beta-estradiol dehydrogenase (aka 17beta-HSD type 1, encoded by HSD17B1) converts estrone to estradiol. Estradiol is the predominant female sex hormone. 17beta-HSD type 3 (aka testosterone 17-beta-dehydrogenase 3, encoded by HSD17B3) catalyses the reduction of androstenedione to testosterone, it also accepts estrogens as substrates. This subgroup also contains a putative steroid dehydrogenase let-767 from Caenorhabditis elegans, mutation in which results in hypersensitivity to cholesterol limitation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 61.85  E-value: 2.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLS----EACGSRVTTVAADLCSIAGV-EQLLASIpSDSEIAGLV 92
Cdd:cd05356   5 VVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAkeieEKYGVETKTIAADFSAGDDIyERIEKEL-EGLDIGILV 83


                ....
gi 32445327  93 HSAG 96
Cdd:cd05356  84 NNVG 87
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 18-231 4.12e-11

tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6,8-tetrahydroxynaphthalene reductase (4HNR) of Magnaporthe grisea and the related 1,3,8-trihydroxynaphthalene reductase (3HNR) are typical members of the SDR family containing the canonical glycine rich NAD(P)-binding site and active site tetrad, and function in fungal melanin biosynthesis. This subgroup also includes an SDR from Norway spruce that may function to protect against both biotic and abitoic stress. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 61.14  E-value: 4.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVF----AVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASipSDSEIAG--- 90
Cdd:cd05362   7 LVTGASRGIGRAIAKRLARDGASVVvnyaSSKAAAEEVVAEIEAAGGKAIAVQADVSDPSQVARLFDA--AEKAFGGvdi 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  91 LVHSAGsLVPLQPYEQIDMNELAEHFRIHVGVPieLFNSLSRDCTVKRMLFIDSYSASNARL---GWGAYSIVKAAAQMA 167
Cdd:cd05362  85 LVNNAG-VMLKKPIAETSEEEFDRMFTVNTKGA--FFVLQEAAKRLRDGGRIINISSSLTAAytpNYGAYAGSKAAVEAF 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32445327 168 ARCAAQELpGTRTIRA---YPGAVNTRIVDAVlASDTQTAStFASMREKGEFAEPEDVARfLVALLV 231
Cdd:cd05362 162 TRVLAKEL-GGRGITVnavAPGPVDTDMFYAG-KTEEAVEG-YAKMSPLGRLGEPEDIAP-VVAFLA 224
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 19-190 5.12e-11

Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a classical SDR which binds NADP. Members of this subgroup contain the YXXXK active site characteristic of SDRs. Also, an upstream Asn residue of the canonical catalytic tetrad is partially conserved in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 60.61  E-value: 5.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  19 VTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRvtTVAADLCSIAGVEQLLASIPSdseIAGLVHSAGSL 98
Cdd:cd11730   3 ILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGAL--ARPADVAAELEVWALAQELGP---LDLLVYAAGAI 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  99 VPlQPYEQIDMNELAEHFRIHV-GVPIELFNSLSRDCTVKRMLFIDSYSASNARLGWGAYSIVKAAAQMAARCAAQELPG 177
Cdd:cd11730  78 LG-KPLARTKPAAWRRILDANLtGAALVLKHALALLAAGARLVFLGAYPELVMLPGLSAYAAAKAALEAYVEVARKEVRG 156

                       170
                ....*....|...
gi 32445327 178 TRTIRAYPGAVNT 190
Cdd:cd11730 157 LRLTLVRPPAVDT 169
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 16-224 5.24e-11

classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a canonical active site triad (and also an active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 60.88  E-value: 5.24e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRGF-RVFAVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPsDSEIagLVHS 94
Cdd:cd05354   5 TVLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPGSAAHLVAKYGDKVVPLRLDVTDPESIKAAAAQAK-DVDV--VINN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  95 AGSLVPLQPYEQIDMNELAEHFRIHVGVPIELFNSLSRdcTVKR-----MLFIDSYSASNARLGWGAYSIVKAAAQMAAR 169
Cdd:cd05354  82 AGVLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFAP--VLKAngggaIVNLNSVASLKNFPAMGTYSASKSAAYSLTQ 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32445327 170 CAAQELP--GTRTIRAYPGAVNTRI---VDAVLASDTQTAS-TFASMREKGEFAEPEDVAR 224
Cdd:cd05354 160 GLRAELAaqGTLVLSVHPGPIDTRMaagAGGPKESPETVAEaVLKALKAGEFHVFPDEMAK 220
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 19-191 8.05e-11

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 60.66  E-value: 8.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   19 VTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLS----EACGSRVTTVAADL--CSIAGVEQLLASIPSD-SEIAGL 91
Cdd:PRK08945  17 VTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYdeieAAGGPQPAIIPLDLltATPQNYQQLADTIEEQfGRLDGV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   92 VHSAGSLVPLQPYEQIDMNELAEHFRIHVGVPIELFNSL------SRDCTVkrmLFIDSYSASNARLGWGAYSIVKAAAQ 165
Cdd:PRK08945  97 LHNAGLLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALlplllkSPAASL---VFTSSSVGRQGRANWGAYAVSKFATE 173

                        170       180
                 ....*....|....*....|....*....
gi 32445327  166 MAARCAAQELPGTrTIRA---YPGAVNTR 191
Cdd:PRK08945 174 GMMQVLADEYQGT-NLRVnciNPGGTRTA 201
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 18-96 8.35e-11

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 60.25  E-value: 8.35e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSE---ACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLVH 93
Cdd:cd05333   4 LVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEeikALGGNAAALEADVSDREAVEALVEKVEAEfGPVDILVN 83


                ...
gi 32445327  94 SAG 96
Cdd:cd05333  84 NAG 86
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 18-230 1.15e-10

classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 59.83  E-value: 1.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIpsDSEIAG---LVHS 94
Cdd:cd08929   4 LVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAM--EEAFGGldaLVNN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  95 AG--------SLVPLQPYEQIDMNELAEHFRIHVGVPielfNSLSRDCTVkrMLFIDSYSASNARLGWGAYSIVKAAAQM 166
Cdd:cd08929  82 AGvgvmkpveELTPEEWRLVLDTNLTGAFYCIHKAAP----ALLRRGGGT--IVNVGSLAGKNAFKGGAAYNASKFGLLG 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32445327 167 AARCAAQELP--GTRTIRAYPGAVNTRIVDAVLASDTQTAstfasmrekgefaePEDVARFLVALL 230
Cdd:cd08929 156 LSEAAMLDLReaNIRVVNVMPGSVDTGFAGSPEGQAWKLA--------------PEDVAQAVLFAL 207
PRK07577 PRK07577
SDR family oxidoreductase;
16-126 1.30e-10

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 59.74  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSV------ELLqslseacgsrvttvAADLCSIAGVEQLLASIPSDSEIA 89
Cdd:PRK07577   5 TVLVTGATKGIGLALSLRLANLGHQVIGIARSAiddfpgELF--------------ACDLADIEQTAATLAQINEIHPVD 70

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 32445327   90 GLVHSAGSLVPlQPYEQIDMNELAEHFRIHVGVPIEL 126
Cdd:PRK07577  71 AIVNNVGIALP-QPLGKIDLAALQDVYDLNVRAAVQV 106
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 18-112 4.11e-10

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; DHB DH (aka 1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase) catalyzes the NAD-dependent conversion of 1,2-dihydroxycyclohexa-3,4-diene carboxylate to a catechol. This subgroup also contains Pseudomonas putida F1 CmtB, 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase, the second enzyme in the pathway for catabolism of p-cumate catabolism. This subgroup shares the glycine-rich NAD-binding motif of the classical SDRs and shares the same catalytic triad; however, the upstream Asn implicated in cofactor binding or catalysis in other SDRs is generally substituted by a Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 58.69  E-value: 4.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSvELLQSLSE---ACGSRVTTVAADLCSIAGVEQLL-ASIPSDSEIAGLVH 93
Cdd:cd08937   8 VVTGAAQGIGRGVAERLAGEGARVLLVDRS-ELVHEVLAeilAAGDAAHVHTADLETYAGAQGVVrAAVERFGRVDVLIN 86

                        90
                ....*....|....*....
gi 32445327  94 SAGSLVPLQPYEQIDMNEL 112
Cdd:cd08937  87 NVGGTIWAKPYEHYEEEQI 105
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
16-147 5.08e-10

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 58.45  E-value: 5.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEAcgSRVTTVAADLCSIAGVEQLLAsipsdsEIAGLVHSA 95
Cdd:COG0451   1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAAL--PGVEFVRGDLRDPEALAAALA------GVDAVVHLA 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 32445327  96 GSLVPlqpyeqiDMNELAEHFRIHVGVPIELFNsLSRDCTVKRMLFIDSYSA 147
Cdd:COG0451  73 APAGV-------GEEDPDETLEVNVEGTLNLLE-AARAAGVKRFVYASSSSV 116
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 18-190 9.06e-10

Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related proteins have a canonical classical SDR nucleotide-binding motif and active site tetrad. They are predicted oxoacyl-(acyl carrier protein/ACP) reductases. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 57.20  E-value: 9.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELL----QSLSEACGSRVTTVAADL--CSIAGVEQLLASIPSD-SEIAG 90
Cdd:cd05340   8 LVTGASDGIGREAALTYARYGATVILLGRNEEKLrqvaDHINEEGGRQPQWFILDLltCTSENCQQLAQRIAVNyPRLDG 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  91 LVHSAGSLVPLQPYEQIDMNELAEHFRIHVGVPIELFNSL------SRDCTVkrmLFIDSYSASNARLGWGAYSIVKAAA 164
Cdd:cd05340  88 VLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALlplllkSDAGSL---VFTSSSVGRQGRANWGAYAVSKFAT 164

                       170       180
                ....*....|....*....|....*....
gi 32445327 165 QMAARCAAQELPGtRTIRA---YPGAVNT 190
Cdd:cd05340 165 EGL*QVLADEYQQ-RNLRVnciNPGGTRT 192
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 19-109 1.13e-09

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 57.36  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   19 VTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQS----LSEACGSRVTTVAADLCSIAGVEQLLASIPsdsEIAGLVHS 94
Cdd:PRK06125  12 ITGASKGIGAAAAEAFAAEGCHLHLVARDADALEAlaadLRAAHGVDVAVHALDLSSPEAREQLAAEAG---DIDILVNN 88

                         90
                 ....*....|....*
gi 32445327   95 AGSlVPLQPYEQIDM 109
Cdd:PRK06125  89 AGA-IPGGGLDDVDD 102
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 16-233 1.61e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 56.65  E-value: 1.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVaaDLCSIAGVEQLLASIPSdseIAGLVHSA 95
Cdd:PRK07060  11 SVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGCEPLRL--DVGDDAAIRAALAAAGA---FDGLVNCA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   96 GSLVpLQPyeQIDMneLAEHFRIHVGVPIELFNSLSRDCTVKR--------MLFIDSYSASNARLGWGAYSIVKAAAQMA 167
Cdd:PRK07060  86 GIAS-LES--ALDM--TAEGFDRVMAVNARGAALVARHVARAMiaagrggsIVNVSSQAALVGLPDHLAYCASKAALDAI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32445327  168 ARCAAQEL--PGTRTIRAYPGAVNTRIVDAVLaSDTQTASTFASMREKGEFAEPEDVARFLVALLVDA 233
Cdd:PRK07060 161 TRVLCVELgpHGIRVNSVNPTVTLTPMAAEAW-SDPQKSGPMLAAIPLGRFAEVDDVAAPILFLLSDA 227
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 16-96 1.63e-09

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 56.62  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSE---ACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGL 91
Cdd:PRK07666   9 NALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEeveAYGVKVVIATADVSDYEEVTAAIEQLKNElGSIDIL 88


                 ....*
gi 32445327   92 VHSAG 96
Cdd:PRK07666  89 INNAG 93
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 19-240 1.76e-09

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 56.80  E-value: 1.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   19 VTGATRGIGRAVAKELAGRGFRVFAVGRS----VELLQSLSEACGSRVTTVAADLCSIAGVEQLLAS-IPSDSEIAGLVH 93
Cdd:PRK12825  11 VTGAARGLGRAIALRLARAGADVVVHYRSdeeaAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAaVERFGRIDILVN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   94 SAG-----SLVPLQP---YEQIDMNELAEHFRIHVGVPIELFNSLSRdctvkrmlfIDSYSASNARLGW---GAYSIVKA 162
Cdd:PRK12825  91 NAGifedkPLADMSDdewDEVIDVNLSGVFHLLRAVVPPMRKQRGGR---------IVNISSVAGLPGWpgrSNYAAAKA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  163 AAQMAARCAAQELpGTRTIRA---YPGAVNTRIVDAVLASDTQTASTFASMrekGEFAEPEDVARFLVALLVDATDELIG 239
Cdd:PRK12825 162 GLVGLTKALAREL-AEYGITVnmvAPGDIDTDMKEATIEEAREAKDAETPL---GRSGTPEDIARAVAFLCSDASDYITG 237


                 .
gi 32445327  240 S 240
Cdd:PRK12825 238 Q 238
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 18-245 2.25e-09

classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187622 [Multi-domain]  Cd Length: 253  Bit Score: 56.27  E-value: 2.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEAC------GSRVTTVAADLCSIAGVEQLLAS-IPSDSEIAG 90
Cdd:cd05364   7 IITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSClqagvsEKKILLVVADLTEEEGQDRIISTtLAKFGRLDI 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  91 LVHSAGSLVPlQPYEQIDMNELAEHFRIHVGVPIELFN------SLSRDCTVKrmlfIDSYSASNARLGWGAYSIVKAAA 164
Cdd:cd05364  87 LVNNAGILAK-GGGEDQDIEEYDKVMNLNLRAVIYLTKlavphlIKTKGEIVN----VSSVAGGRSFPGVLYYCISKAAL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327 165 QMAARCAAQELP--GTRTIRAYPGAVNTRIVDAVLASDTQTASTFASMREK---GEFAEPEDVARFLVALLVDATDELIG 239
Cdd:cd05364 162 DQFTRCTALELApkGVRVNSVSPGVIVTGFHRRMGMPEEQYIKFLSRAKEThplGRPGTVDEVAEAIAFLASDASSFITG 241


                ....*.
gi 32445327 240 SRDVFD 245
Cdd:cd05364 242 QLLPVD 247
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 18-96 2.27e-09

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 56.52  E-value: 2.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLS---EACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLVH 93
Cdd:PRK12939  11 LVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAaalEAAGGRAHAIAADLADPASVQRFFDAAAAAlGGLDGLVN 90


                 ...
gi 32445327   94 SAG 96
Cdd:PRK12939  91 NAG 93
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 19-103 4.76e-09

bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase YdfG;


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 55.53  E-value: 4.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   19 VTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLVHSAGS 97
Cdd:PRK10538   5 VTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEwRNIDVLVNNAGL 84


                 ....*.
gi 32445327   98 LVPLQP 103
Cdd:PRK10538  85 ALGLEP 90
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 16-126 4.85e-09

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187602 [Multi-domain]  Cd Length: 253  Bit Score: 55.36  E-value: 4.85e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEAC---GSRVTTVAADLCSIAGVEQLL-ASIPSDSEIAGL 91
Cdd:cd05344   3 VALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELragGAGVLAVVADLTDPEDIDRLVeKAGDAFGRVDIL 82

                        90       100       110
                ....*....|....*....|....*....|....*
gi 32445327  92 VHSAGSlVPLQPYEQIDMNELAEHFRIHVGVPIEL 126
Cdd:cd05344  83 VNNAGG-PPPGPFAELTDEDWLEAFDLKLLSVIRI 116
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 16-239 5.35e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 55.58  E-value: 5.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSR-----VTTVAADLCSIAGVEQLLASIPS-DSEIA 89
Cdd:PRK05875   9 TYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIEALkgagaVRYEPADVTDEDQVARAVDAATAwHGRLH 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   90 GLVHSAGSLVPLQPYEQIDMNELAEHFRIHVGVPIELFNSLSRDCTVK---RMLFIDSYSASNARLGWGAYSIVKAAAQM 166
Cdd:PRK05875  89 GVVHCAGGSETIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGgggSFVGISSIAASNTHRWFGAYGVTKSAVDH 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32445327  167 AARCAAQELpGTRTIRA---YPGAVNTRIVDAVLASDTQTAStFASMREKGEFAEPEDVARFLVALLVDATDELIG 239
Cdd:PRK05875 169 LMKLAADEL-GPSWVRVnsiRPGLIRTDLVAPITESPELSAD-YRACTPLPRVGEVEDVANLAMFLLSDAASWITG 242
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 18-96 6.86e-09

11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human 11beta_HSD1 catalyzes the NADP(H)-dependent interconversion of cortisone and cortisol. This subgroup also includes human dehydrogenase/reductase SDR family member 7C (DHRS7C) and DHRS7B. These proteins have the GxxxGxG nucleotide binding motif and S-Y-K catalytic triad characteristic of the SDRs, but have an atypical C-terminal domain that contributes to homodimerization contacts. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 54.90  E-value: 6.86e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGS----RVTTVAADLCSIAGVEQLLASIPSD-SEIAGLV 92
Cdd:cd05332   7 IITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLElgapSPHVVPLDMSDLEDAEQVVEEALKLfGGLDILI 86


                ....
gi 32445327  93 HSAG 96
Cdd:cd05332  87 NNAG 90
PRK07775 PRK07775
SDR family oxidoreductase;
18-228 7.32e-09

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 55.15  E-value: 7.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSE---ACGSRVTTVAADLCSIAGVEQLLA-SIPSDSEIAGLVH 93
Cdd:PRK07775  14 LVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDkirADGGEAVAFPLDVTDPDSVKSFVAqAEEALGEIEVLVS 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   94 SAGSLVPLQPYEqIDMNELAEHFRIHVGVPIELFNSLSRDCTVKR---MLFIDSYSASNARLGWGAYSIVKAAAQMAARC 170
Cdd:PRK07775  94 GAGDTYFGKLHE-ISTEQFESQVQIHLVGANRLATAVLPGMIERRrgdLIFVGSDVALRQRPHMGAYGAAKAGLEAMVTN 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32445327  171 AAQELPGTrTIRA---YPGAVNTRIVDAVLASDTQTA----STFASMREkGEFAEPEDVARFLVA 228
Cdd:PRK07775 173 LQMELEGT-GVRAsivHPGPTLTGMGWSLPAEVIGPMledwAKWGQARH-DYFLRASDLARAITF 235
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 18-231 7.99e-09

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 54.75  E-value: 7.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVfAVG------RSVELLQSLsEACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAG 90
Cdd:PRK12937   9 IVTGASRGIGAAIARRLAADGFAV-AVNyagsaaAADELVAEI-EAAGGRAIAVQADVADAAAVTRLFDAAETAfGRIDV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   91 LVHSAGSLvPLQPYEQIDMNELAEHFRIHV-GVPIELFNSLSRDCTVKRMLFIDSYSASNARLGWGAYSIVKAAAQMAAR 169
Cdd:PRK12937  87 LVNNAGVM-PLGTIADFDLEDFDRTIATNLrGAFVVLREAARHLGQGGRIINLSTSVIALPLPGYGPYAASKAAVEGLVH 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32445327  170 CAAQELPGtRTIRA---YPGAVNTRIVDAvlASDTQTASTFASMREKGEFAEPEDVARfLVALLV 231
Cdd:PRK12937 166 VLANELRG-RGITVnavAPGPVATELFFN--GKSAEQIDQLAGLAPLERLGTPEEIAA-AVAFLA 226
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 16-96 9.52e-09

Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 54.40  E-value: 9.52e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGsRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLVHS 94
Cdd:COG3967   7 TILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAANP-GLHTIVLDVADPASIAALAEQVTAEfPDLNVLINN 85


                ..
gi 32445327  95 AG 96
Cdd:COG3967  86 AG 87
PRK09134 PRK09134
SDR family oxidoreductase;
6-126 1.48e-08

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 54.16  E-value: 1.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327    6 SWKSNMQAIPTYVVTGATRGIGRAVAKELAGRGFRVfAV--GRSVELLQSLSE---ACGSRVTTVAADLCSIAGVEQLLA 80
Cdd:PRK09134   1 SPPMSMAAPRAALVTGAARRIGRAIALDLAAHGFDV-AVhyNRSRDEAEALAAeirALGRRAVALQADLADEAEVRALVA 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 32445327   81 -SIPSDSEIAGLVHSAgSLVPLQPYEQIDMNELAEHFRIHVGVPIEL 126
Cdd:PRK09134  80 rASAALGPITLLVNNA-SLFEYDSAASFTRASWDRHMATNLRAPFVL 125
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 8-77 1.54e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 54.54  E-value: 1.54e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32445327    8 KSNMQAIPTYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLS---EACGSRVTTVAADLCSIAGVEQ 77
Cdd:PRK07109   2 MLKPIGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAaeiRAAGGEALAVVADVADAEAVQA 74
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 18-96 2.04e-08

3-ketoacyl-(acyl-carrier-protein) reductase; Validated


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 53.66  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRS----VELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLV 92
Cdd:PRK05557   9 LVTGASRGIGRAIAERLAAQGANVVINYASseagAEALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEfGGVDILV 88


                 ....
gi 32445327   93 HSAG 96
Cdd:PRK05557  89 NNAG 92
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 16-114 2.97e-08

ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the single KR domain of SpiF, the first KR domains of SpiE,-G,H,-I,and #J, the third KR domain of SpiG, and the second KR domain of SpiH. The second KR domains of SpiE,-G, I, and #J, and the KR domains of SpiD, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187655 [Multi-domain]  Cd Length: 480  Bit Score: 53.71  E-value: 2.97e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRG-FRVFAVGRS-------VELLQSLSEAcGSRVTTVAADLCSIAGVEQLLASIPSDSE 87
Cdd:cd08952 232 TVLVTGGTGALGAHVARWLARRGaEHLVLTSRRgpdapgaAELVAELTAL-GARVTVAACDVADRDALAALLAALPAGHP 310

                        90       100
                ....*....|....*....|....*..
gi 32445327  88 IAGLVHSAGsLVPLQPYEQIDMNELAE 114
Cdd:cd08952 311 LTAVVHAAG-VLDDGPLDDLTPERLAE 336
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 18-106 3.06e-08

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 53.02  E-value: 3.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRS--VELLQSLSEACGSRVTTVAADLCSIAGVEQLLAS-IPSDSEIAGLVHS 94
Cdd:PRK12823  12 VVTGAAQGIGRGVALRAAAEGARVVLVDRSelVHEVAAELRAAGGEALALTADLETYAGAQAAMAAaVEAFGRIDVLINN 91

                         90
                 ....*....|..
gi 32445327   95 AGSLVPLQPYEQ 106
Cdd:PRK12823  92 VGGTIWAKPFEE 103
PRK06484 PRK06484
short chain dehydrogenase; Validated
 18-250 3.19e-08

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 53.70  E-value: 3.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLVHSAG 96
Cdd:PRK06484   9 LVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREfGRIDVLVNNAG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   97 SLVPlQPYEQIDMNelAEHFRIHVGVPIELFNSLSRDcTVKRMLF---------IDSYSASNARLGWGAYSIVKAAAQMA 167
Cdd:PRK06484  89 VTDP-TMTATLDTT--LEEFARLQAINLTGAYLVARE-ALRLMIEqghgaaivnVASGAGLVALPKRTAYSASKAAVISL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  168 ARCAAQELP--GTRTIRAYPGAVNTRIVDAVLASDTQTASTFASMREKGEFAEPEDVARFLVALLVDATDELIGSRDVFD 245
Cdd:PRK06484 165 TRSLACEWAakGIRVNAVLPGYVRTQMVAELERAGKLDPSAVRSRIPLGRLGRPEEIAEAVFFLASDQASYITGSTLVVD 244

                        250
                 ....*....|
gi 32445327  246 -----YNNPG 250
Cdd:PRK06484 245 ggwtvYGGSG 254
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 18-240 3.51e-08

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 52.88  E-value: 3.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVE-LLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLVHSA 95
Cdd:PRK12828  11 AITGGFGGLGRATAAWLAARGARVALIGRGAApLSQTLPGVPADALRIGGIDLVDPQAARRAVDEVNRQfGRLDALVNIA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   96 GSLvPLQPYEQIDMNELAEHFRIHVGVPIELFNSLSRDCT---VKRMLFIDSYSASNARLGWGAYSIVKAAAQMAARCAA 172
Cdd:PRK12828  91 GAF-VWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTasgGGRIVNIGAGAALKAGPGMGAYAAAKAGVARLTEALA 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  173 QELpGTRTIRaypgavntriVDAVLAS--DTQTASTFASMREKGEFAEPEDVARFLVALLVDATDELIGS 240
Cdd:PRK12828 170 AEL-LDRGIT----------VNAVLPSiiDTPPNRADMPDADFSRWVTPEQIAAVIAFLLSDEAQAITGA 228
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 16-126 4.60e-08

classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka Tyrosine-dependent oxidoreductases) are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 52.31  E-value: 4.60e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSrVTTVAADLCSIAGVEQLLASIPSD-SEIAGLVHS 94
Cdd:cd05370   7 TVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPN-IHTIVLDVGDAESVEALAEALLSEyPNLDILINN 85

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 32445327  95 AGSlvpLQPYE----QIDMNELAEHFRIHVGVPIEL 126
Cdd:cd05370  86 AGI---QRPIDlrdpASDLDKADTEIDTNLIGPIRL 118
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 18-232 4.90e-08

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 52.54  E-value: 4.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVG-----RSVELLQSLSEAcGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGL 91
Cdd:PRK05565   9 IVTGASGGIGRAIAELLAKEGAKVVIAYdineeAAQELLEEIKEE-GGDAIAVKADVSSEEDVENLVEQIVEKfGKIDIL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   92 VHSAG--SLVPLqpyEQIDMNELAEHFRIHVGVPIElfnsLSRDCtVKRML--------FIDS----YSASNARLgwgaY 157
Cdd:PRK05565  88 VNNAGisNFGLV---TDMTDEEWDRVIDVNLTGVML----LTRYA-LPYMIkrksgvivNISSiwglIGASCEVL----Y 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  158 SIVKAAAQMAARCAAQELP--GTRTIRAYPGAVNTRIvdavlasdtqtASTFASMREK--------GEFAEPEDVARfLV 227
Cdd:PRK05565 156 SASKGAVNAFTKALAKELApsGIRVNAVAPGAIDTEM-----------WSSFSEEDKEglaeeiplGRLGKPEEIAK-VV 223


                 ....*
gi 32445327  228 ALLVD 232
Cdd:PRK05565 224 LFLAS 228
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 11-96 5.51e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 52.60  E-value: 5.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   11 MQAIPTYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLseacgSRVTTVAADLCSIAGVEQLLASIpsdSEIAG 90
Cdd:PRK06179   1 MSNSKVALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAAPI-----PGVELLELDVTDDASVQAAVDEV---IARAG 72

                         90
                 ....*....|
gi 32445327   91 ----LVHSAG 96
Cdd:PRK06179  73 ridvLVNNAG 82
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 18-96 6.53e-08

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 51.97  E-value: 6.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELL---QSLSEACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLVH 93
Cdd:cd05347   9 LVTGASRGIGFGIASGLAEAGANIVINSRNEEKAeeaQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDfGKIDILVN 88


                ...
gi 32445327  94 SAG 96
Cdd:cd05347  89 NAG 91
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
 9-98 6.78e-08

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); Ketoreductase, a module of the multidomain polyketide synthase, has 2 subdomains, each corresponding to a short-chain dehydrogenases/reductase (SDR) family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerizes but is composed of 2 subdomains, each resembling an SDR monomer. In some instances, as in porcine FAS, an enoyl reductase (a Rossman fold NAD binding domain of the MDR family) module is inserted between the sub-domains. The active site resembles that of typical SDRs, except that the usual positions of the catalytic asparagine and tyrosine are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular polyketide synthases are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) fatty acid synthase. In some instances, such as porcine FAS , an enoyl reductase module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER). Polyketide syntheses also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes the KR domain of the Lyngbya majuscule Jam J, -K, and #L which are encoded on the jam gene cluster and are involved in the synthesis of the Jamaicamides (neurotoxins); Lyngbya majuscule Jam P belongs to a different KR_FAS_SDR_x subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187658 [Multi-domain]  Cd Length: 376  Bit Score: 52.67  E-value: 6.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   9 SNMQAIPTYVVTGATRGIGRAVAKELAGRGFR-VFAVGRS------VELLQSLsEACGSRVTTVAADLCSIAGVEQLLAS 81
Cdd:cd08955 144 RPLRPDATYLITGGLGGLGLLVAEWLVERGARhLVLTGRRapsaaaRQAIAAL-EEAGAEVVVLAADVSDRDALAAALAQ 222

                        90
                ....*....|....*...
gi 32445327  82 IPSDS-EIAGLVHSAGSL 98
Cdd:cd08955 223 IRASLpPLRGVIHAAGVL 240
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 18-76 8.03e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 52.28  E-value: 8.03e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACG--SRVTTVAADLCSIAGVE 76
Cdd:PRK05872  13 VVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGgdDRVLTVVADVTDLAAMQ 73
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 18-98 8.37e-08

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 51.88  E-value: 8.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVAADLCSIAG---VEQLLASIPSD-SEIAGLVH 93
Cdd:PRK08217   9 VITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGTEVRGYAANVTDeedVEATFAQIAEDfGQLNGLIN 88


                 ....*
gi 32445327   94 SAGSL 98
Cdd:PRK08217  89 NAGIL 93
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 16-80 9.51e-08

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 51.38  E-value: 9.51e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEAcgsRVTTVAADLCSIAGVEQLLA 80
Cdd:COG0702   1 KILVTGATGFIGRRVVRALLARGHPVRALVRDPEKAAALAAA---GVEVVQGDLDDPESLAAALA 62
PRK07201 PRK07201
SDR family oxidoreductase;
18-82 9.52e-08

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 52.65  E-value: 9.52e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLS---EACGSRVTTVAADLCSIAGVEQLLASI 82
Cdd:PRK07201 375 LITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVaeiRAKGGTAHAYTCDLTDSAAVDHTVKDI 442
PRK06101 PRK06101
SDR family oxidoreductase;
16-83 1.02e-07

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 51.41  E-value: 1.02e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLsEACGSRVTTVAADLCSIAGVEQLLASIP 83
Cdd:PRK06101   3 AVLITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDEL-HTQSANIFTLAFDVTDHPGTKAALSQLP 69
PRK08264 PRK08264
SDR family oxidoreductase;
16-224 1.13e-07

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 51.43  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFR-VFAVGRSVELLQSLseacGSRVTTVAADLCSIAGVEQlLASIPSDSEIagLVHS 94
Cdd:PRK08264   8 VVLVTGANRGIGRAFVEQLLARGAAkVYAAARDPESVTDL----GPRVVPLQLDVTDPASVAA-AAEAASDVTI--LVNN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   95 AGSLVPLQPYEQIDMNELAEHFRIHV-------------------GVPIELFNSLSrdctVKRMLFIDSYSASNArlgwG 155
Cdd:PRK08264  81 AGIFRTGSLLLEGDEDALRAEMETNYfgplamarafapvlaanggGAIVNVLSVLS----WVNFPNLGTYSASKA----A 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32445327  156 AYSIVKAAAQmaarcaaqELP--GTRTIRAYPGAVNTRIVDAVLAsdtqtastfasmrEKgefAEPEDVAR 224
Cdd:PRK08264 153 AWSLTQALRA--------ELApqGTRVLGVHPGPIDTDMAAGLDA-------------PK---ASPADVAR 199
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 15-96 1.25e-07

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 51.12  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   15 PTYVVTGATRGIGRAVAKELAGRGFRVFAVGRS-----VELLQSLSEAcGSRVTTVAADLCSIAGVEQLLASIPSDS-EI 88
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAINDRPddeelAATQQELRAL-GVEVIFFPADVADLSAHEAMLDAAQAAWgRI 81


                 ....*...
gi 32445327   89 AGLVHSAG 96
Cdd:PRK12745  82 DCLVNNAG 89
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 19-238 1.64e-07

1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup contains classical SDR proteins, including members identified as 1-cyclohexenylcarbonyl coenzyme A reductase. ChcA of Streptomyces collinus is implicated in the final reduction step of shikimic acid to ansatrienin. ChcA shows sequence similarity to the SDR family of NAD-binding proteins, but it lacks the conserved Tyr of the characteristic catalytic site. This subgroup also contains the NADH-dependent enoyl-[acyl-carrier-protein(ACP)] reductase FabL from Bacillus subtilis. This enzyme participates in bacterial fatty acid synthesis, in type II fatty-acid synthases and catalyzes the last step in each elongation cycle. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187617 [Multi-domain]  Cd Length: 242  Bit Score: 50.81  E-value: 1.64e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  19 VTGATRGIGRAVAKELAGRGFRVFAVGR-SVELLQSLSEAC---GSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLVH 93
Cdd:cd05359   3 VTGGSRGIGKAIALRLAERGADVVINYRkSKDAAAEVAAEIeelGGKAVVVRADVSQPQDVEEMFAAVKERfGRLDVLVS 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  94 SA--GSLVPLQPYE------QIDMNELAEHFRIHVGVPielfnsLSRDCTVKRMLFIDSYSASNARLGWGAYSIVKAAAQ 165
Cdd:cd05359  83 NAaaGAFRPLSELTpahwdaKMNTNLKALVHCAQQAAK------LMRERGGGRIVAISSLGSIRALPNYLAVGTAKAALE 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32445327 166 MAARCAAQELpGTRTIRA---YPGAVNTRIVDAVL-ASDTQTASTFASMRekGEFAEPEDVARfLVALLVDATDELI 238
Cdd:cd05359 157 ALVRYLAVEL-GPRGIRVnavSPGVIDTDALAHFPnREDLLEAAAANTPA--GRVGTPQDVAD-AVGFLCSDAARMI 229
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 18-96 1.89e-07

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 50.75  E-value: 1.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEAcGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLVHSAG 96
Cdd:cd05371   6 VVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAKL-GDNCRFVPVDVTSEKDVKAALALAKAKfGRLDIVVNCAG 84
FabG-like PRK07231
SDR family oxidoreductase;
16-239 2.10e-07

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 50.60  E-value: 2.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEA--CGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLV 92
Cdd:PRK07231   7 VAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEilAGGRAIAVAADVSDEADVEAAVAAALERfGSVDILV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   93 HSAGSLVPLQPYEQIDMNELAEHFRIHVGVPIelfnsLSRDCTVKRM--------LFIDSYSASNARLGWGAYSIVKAAA 164
Cdd:PRK07231  87 NNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPY-----LWTQAAVPAMrgegggaiVNVASTAGLRPRPGLGWYNASKGAV 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32445327  165 QMAARCAAQELpGTRTIRA---YPGAVNTRIVDAVLASDTQTA-STFASMREKGEFAEPEDVARFLVALLVDATDELIG 239
Cdd:PRK07231 162 ITLTKALAAEL-GPDKIRVnavAPVVVETGLLEAFMGEPTPENrAKFLATIPLGRLGTPEDIANAALFLASDEASWITG 239
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 18-108 2.18e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 50.43  E-value: 2.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSDS-EIAGLVHSAG 96
Cdd:PRK06841  19 VVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVISAFgRIDILVNSAG 98

                         90
                 ....*....|..
gi 32445327   97 sLVPLQPYEQID 108
Cdd:PRK06841  99 -VALLAPAEDVS 109
PRK06947 PRK06947
SDR family oxidoreductase;
16-240 2.32e-07

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 50.57  E-value: 2.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRV---FAVGR-SVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAG 90
Cdd:PRK06947   4 VVLITGASRGIGRATAVLAAARGWSVginYARDAaAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAfGRLDA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   91 LVHSAGSLVPLQPYEQIDMNELAEHFRIHVG----VPIELFNSLSRDCTVKRMLFIDSYSASnARLG----WGAYSIVKA 162
Cdd:PRK06947  84 LVNNAGIVAPSMPLADMDAARLRRMFDTNVLgaylCAREAARRLSTDRGGRGGAIVNVSSIA-SRLGspneYVDYAGSKG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  163 AAQMAARCAAQEL--PGTRTIRAYPGAVNTRIvdavLASDTQT--ASTFASMREKGEFAEPEDVARFLVALLVDATDELI 238
Cdd:PRK06947 163 AVDTLTLGLAKELgpHGVRVNAVRPGLIETEI----HASGGQPgrAARLGAQTPLGRAGEADEVAETIVWLLSDAASYVT 238


                 ..
gi 32445327  239 GS 240
Cdd:PRK06947 239 GA 240
PRK06181 PRK06181
SDR family oxidoreductase;
18-81 3.41e-07

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 49.98  E-value: 3.41e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEAC---GSRVTTVAADLCSIAGVEQLLAS 81
Cdd:PRK06181   5 IITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELadhGGEALVVPTDVSDAEACERLIEA 71
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 18-232 3.45e-07

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This subgroup includes human DHRS1 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 50.14  E-value: 3.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLS----EACGSRVTTVAADLCSIAGVEQLLASIpsDSEIAG--- 90
Cdd:cd09763   7 LVTGASRGIGRGIALQLGEAGATVYITGRTILPQLPGTaeeiEARGGKCIPVRCDHSDDDEVEALFERV--AREQQGrld 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  91 -LVHSAGSLVplqpyeQIDMNELAEHF----------RIHVGVPIELFNS-----LSRDCTVKRMLFIDSYSASNARLGW 154
Cdd:cd09763  85 iLVNNAYAAV------QLILVGVAKPFweepptiwddINNVGLRAHYACSvyaapLMVKAGKGLIVIISSTGGLEYLFNV 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327 155 gAYSIVKAAAQMAARCAAQELP--GTRTIRAYPGAVNTRIVDAVLASDtqTASTFASMREKGEFAE-PEDVARFLVALLV 231
Cdd:cd09763 159 -AYGVGKAAIDRMAADMAHELKphGVAVVSLWPGFVRTELVLEMPEDD--EGSWHAKERDAFLNGEtTEYSGRCVVALAA 235


                .
gi 32445327 232 D 232
Cdd:cd09763 236 D 236
PRK05866 PRK05866
SDR family oxidoreductase;
18-96 7.00e-07

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 49.35  E-value: 7.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSE---ACGSRVTTVAADLCSIAGVEQLLASIpsDSEIAG---L 91
Cdd:PRK05866  44 LLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADritRAGGDAMAVPCDLSDLDAVDALVADV--EKRIGGvdiL 121


                 ....*
gi 32445327   92 VHSAG 96
Cdd:PRK05866 122 INNAG 126
PRK07102 PRK07102
SDR family oxidoreductase;
11-133 7.55e-07

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 48.77  E-value: 7.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   11 MQAIptyVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEAC----GSRVTTVAADLCSIAGVEQLLASIPSDS 86
Cdd:PRK07102   1 MKKI---LIIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLrargAVAVSTHELDILDTASHAAFLDSLPALP 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 32445327   87 EIAGLVHsaGSLvPLQPYEQIDMNELAEHFRIHVGVPIELFNSLSRD 133
Cdd:PRK07102  78 DIVLIAV--GTL-GDQAACEADPALALREFRTNFEGPIALLTLLANR 121
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 18-78 7.58e-07

classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a canonical active site triad (and also active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 48.92  E-value: 7.58e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLS---EACGSRVTTVAADLCSIAGVEQL 78
Cdd:cd05360   4 VITGASSGIGRATALAFAERGAKVVLAARSAEALHELArevRELGGEAIAVVADVADAAQVERA 67
PRK06182 PRK06182
short chain dehydrogenase; Validated
 15-96 1.09e-06

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 48.42  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   15 PTYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEAcgsRVTTVAADLCSIAGVEQLLASIPSDS-EIAGLVH 93
Cdd:PRK06182   4 KVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLASL---GVHPLSLDVTDEASIKAAVDTIIAEEgRIDVLVN 80


                 ...
gi 32445327   94 SAG 96
Cdd:PRK06182  81 NAG 83
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 18-96 1.10e-06

Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR with a characteristic NAD-binding pattern and active site tetrad. Aromatic polyketides include various aromatic compounds of pharmaceutical interest. Polyketide KR, part of the type II polyketide synthase (PKS) complex, is comprised of stand-alone domains that resemble the domains found in fatty acid synthase and multidomain type I PKS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 48.69  E-value: 1.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQS----LSEAcGSRVTTVAADLCSIAGVEQLLAS-IPSDSEIAGLV 92
Cdd:cd08945   7 LVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATtvkeLREA-GVEADGRTCDVRSVPEIEALVAAaVARYGPIDVLV 85


                ....
gi 32445327  93 HSAG 96
Cdd:cd08945  86 NNAG 89
PRK07074 PRK07074
SDR family oxidoreductase;
16-97 1.31e-06

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 48.23  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGS-RVTTVAADLCSIAGVEQLLASIPSD-SEIAGLVH 93
Cdd:PRK07074   4 TALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDaRFVPVACDLTDAASLAAALANAAAErGPVDVLVA 83


                 ....
gi 32445327   94 SAGS 97
Cdd:PRK07074  84 NAGA 87
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 15-68 1.66e-06

SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are putative oxidoreductases belonging to the larger SDR family. All members occur in genomes that encode a cassette for the biosynthesis of mycofactocin, a proposed electron carrier of a novel redox pool. Characterized members of this family are described as NDMA-dependent, meaning that a blue aniline dye serving as an artificial electron acceptor is required for members of this family to cycle in vitro, since the bound NAD residue is not exchangeable. This family resembles TIGR03971 most closely in the N-terminal region, consistent with the published hypothesis of NAD interaction with mycofactocin. See EC 1.1.99.36. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 48.09  E-value: 1.66e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32445327    15 PTYVVTGATRGIGRAVAKELAGRGFRVFAVGR------------SVELLQSLSEACGSRVTTVAAD 68
Cdd:TIGR04504   2 RVALVTGAARGIGAATVRRLAADGWRVVAVDLcaddpavgyplaTRAELDAVAAACPDQVLPVIAD 67
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 16-77 1.78e-06

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 48.11  E-value: 1.78e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQ 77
Cdd:PRK08263   5 VWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTDRAAVFA 66
PRK07814 PRK07814
SDR family oxidoreductase;
18-239 2.03e-06

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 47.85  E-value: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSE---ACGSRVTTVAADLCSIAGVEQLL-ASIPSDSEIAGLVH 93
Cdd:PRK07814  14 VVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEqirAAGRRAHVVAADLAHPEATAGLAgQAVEAFGRLDIVVN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   94 SAGSLVPlQPYEQIDMNELAEHFRIHVGVPielfNSLSRdCTVKRML---------FIDSYSASNARLGWGAYSIVKAAA 164
Cdd:PRK07814  94 NVGGTMP-NPLLSTSTKDLADAFTFNVATA----HALTV-AAVPLMLehsgggsviNISSTMGRLAGRGFAAYGTAKAAL 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32445327  165 QMAARCAAQEL-PGTRTIRAYPGAVNTRIVDAVLASDT--QTASTFASMREKGefaEPEDVARFLVALLVDATDELIG 239
Cdd:PRK07814 168 AHYTRLAALDLcPRIRVNAIAPGSILTSALEVVAANDElrAPMEKATPLRRLG---DPEDIAAAAVYLASPAGSYLTG 242
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 18-80 2.10e-06

human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These proteins are members of the SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187601 [Multi-domain]  Cd Length: 250  Bit Score: 47.51  E-value: 2.10e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEAC-GSRVTTVAADLCSIAGVEQLLA 80
Cdd:cd05343  10 LVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECqSAGYPTLFPYQCDLSNEEQILS 73
PRK07326 PRK07326
SDR family oxidoreductase;
19-123 2.65e-06

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 47.31  E-value: 2.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   19 VTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGS--RVTTVAADLCSIAGVEQLLASIpsDSEIAGL---VH 93
Cdd:PRK07326  11 ITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNkgNVLGLAADVRDEADVQRAVDAI--VAAFGGLdvlIA 88

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 32445327   94 SAG--------SLVPLQPYEQIDMNELAEHFRIHVGVP 123
Cdd:PRK07326  89 NAGvghfapveELTPEEWRLVIDTNLTGAFYTIKAAVP 126
NAD_binding_10 pfam13460
NAD(P)H-binding;
21-80 2.93e-06

NAD(P)H-binding;


Pssm-ID: 463885 [Multi-domain]  Cd Length: 183  Bit Score: 46.44  E-value: 2.93e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327    21 GATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEAcgSRVTTVAADLCSIAGVEQLLA 80
Cdd:pfam13460   1 GATGKIGRLLVKQLLARGHEVTALVRNPEKLADLEDH--PGVEVVDGDVLDPDDLAEALA 58
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 18-82 2.99e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 47.31  E-value: 2.99e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASI 82
Cdd:PRK08265  10 IVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGERARFIATDITDDAAIERAVATV 74
PRK07806 PRK07806
SDR family oxidoreductase;
16-82 3.08e-06

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 47.02  E-value: 3.08e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFAV-----GRSVELLQSLSEAcGSRVTTVAADLCSIAGVEQLLASI 82
Cdd:PRK07806   8 TALVTGSSRGIGADTAKILAGAGAHVVVNyrqkaPRANKVVAEIEAA-GGRASAVGADLTDEESVAALMDTA 78
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 18-228 3.14e-06

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 46.99  E-value: 3.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRG--FRVFAVGRSVELLQSLSE--ACGSRVTTVAADLCSIAGVEQLLASIPSD-------S 86
Cdd:PRK12747   8 LVTGASRGIGRAIAKRLANDGalVAIHYGNRKEEAEETVYEiqSNGGSAFSIGANLESLHGVEALYSSLDNElqnrtgsT 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   87 EIAGLVHSAGsLVPLQPYEQIDMNELAEHFRIHVGVPIELFN-SLSRDCTVKRMLFIDSYSASNARLGWGAYSIVKAAAQ 165
Cdd:PRK12747  88 KFDILINNAG-IGPGAFIEETTEQFFDRMVSVNAKAPFFIIQqALSRLRDNSRIINISSAATRISLPDFIAYSMTKGAIN 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32445327  166 MAARCAAQELpGTRTIRA---YPGAVNTRIvDAVLASD---TQTASTFASMREKGEFAEPEDVARFLVA 228
Cdd:PRK12747 167 TMTFTLAKQL-GARGITVnaiLPGFIKTDM-NAELLSDpmmKQYATTISAFNRLGEVEDIADTAAFLAS 233
YwnB COG2910
Putative NADH-flavin reductase [General function prediction only];
18-80 3.35e-06

Putative NADH-flavin reductase [General function prediction only];


Pssm-ID: 442154 [Multi-domain]  Cd Length: 205  Bit Score: 46.39  E-value: 3.35e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEacgsRVTTVAADLCSIAGVEQLLA 80
Cdd:COG2910   3 AVIGATGRVGSLIVREALARGHEVTALVRNPEKLPDEHP----GLTVVVGDVLDPAAVAEALA 61
PRK07041 PRK07041
SDR family oxidoreductase;
18-100 3.57e-06

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 46.57  E-value: 3.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGS--RVTTVAADLCSIAGVEQLLASIPS-DSEIAGLVHS 94
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGgaPVRTAALDITDEAAVDAFFAEAGPfDHVVITAADT 80


                 ....*.
gi 32445327   95 AGSLVP 100
Cdd:PRK07041  81 PGGPVR 86
PRK09242 PRK09242
SDR family oxidoreductase;
7-96 3.72e-06

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 47.05  E-value: 3.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327    7 WKSNMQaipTYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSL-----SEACGSRVTTVAADLCSIAGVEQLLAS 81
Cdd:PRK09242   5 WRLDGQ---TALITGASKGIGLAIAREFLGLGADVLIVARDADALAQArdelaEEFPEREVHGLAADVSDDEDRRAILDW 81

                         90
                 ....*....|....*.
gi 32445327   82 IPSDS-EIAGLVHSAG 96
Cdd:PRK09242  82 VEDHWdGLHILVNNAG 97
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
18-96 3.74e-06

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 46.68  E-value: 3.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVEL----LQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLV 92
Cdd:PRK12824   6 LVTGAKRGIGSAIARELLNDGYRVIATYFSGNDcakdWFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEEeGPVDILV 85


                 ....
gi 32445327   93 HSAG 96
Cdd:PRK12824  86 NNAG 89
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 16-120 3.75e-06

human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical SDR subgroup includes human type 1 17beta-HSD, human retinol dehydrogenase 8, zebrafish photoreceptor associated retinol dehydrogenase type 2, and a chicken ovary-specific 17beta-hydroxysteroid dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 47.07  E-value: 3.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  16 TYVVTGATRGIGRAVAKELA---GRGFRVFAVGRSV----ELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPsDSEI 88
Cdd:cd09806   2 VVLITGCSSGIGLHLAVRLAsdpSKRFKVYATMRDLkkkgRLWEAAGALAGGTLETLQLDVCDSKSVAAAVERVT-ERHV 80

                        90       100       110
                ....*....|....*....|....*....|..
gi 32445327  89 AGLVHSAGsLVPLQPYEQIDMNELAEHFRIHV 120
Cdd:cd09806  81 DVLVCNAG-VGLLGPLEALSEDAMASVFDVNV 111
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 18-144 3.93e-06

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 46.52  E-value: 3.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327    18 VVTGATRGIGRAVAKELAGRGFRVFAVGRsveLLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSDseiaGLVHSAG- 96
Cdd:pfam01370   2 LVTGATGFIGSHLVRRLLEKGYEVIGLDR---LTSASNTARLADLRFVEGDLTDRDALEKLLADVRPD----AVIHLAAv 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 32445327    97 SLVPLqpyeqiDMNELAEHFRIHVGVPIELFNSLsRDCTVKRMLFIDS 144
Cdd:pfam01370  75 GGVGA------SIEDPEDFIEANVLGTLNLLEAA-RKAGVKRFLFASS 115
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 16-157 4.38e-06

2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 46.80  E-value: 4.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLseacgsRVTTVAADLCSIAGVEQLLASIPSDSE-IAGLVHS 94
Cdd:PRK08220  10 TVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQEDY------PFATFVLDVSDAAAVAQVCQRLLAETGpLDVLVNA 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32445327   95 AGSLvPLQPYEQIDMNELAEHFRIHVGVPIELFNSLSRDCTVKR---MLFIDSYSASNARLGWGAY 157
Cdd:PRK08220  84 AGIL-RMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRsgaIVTVGSNAAHVPRIGMAAY 148
KR_3_FAS_SDR_x cd08956
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); ...
 16-98 4.41e-06

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta- ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the second KR domains of SpiE,-G, I, and -J, both KR domains of SpiD, and the third KR domain of SpiH. The single KR domain of SpiF, the first and second KR domains of SpiH, the first KR domains of SpiE,-G,- I, and -J, and the third KR domain of SpiG, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187659 [Multi-domain]  Cd Length: 448  Bit Score: 47.26  E-value: 4.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRG--FRVFAVGRS------VELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSDSE 87
Cdd:cd08956 195 TVLITGGTGTLGALLARHLVTEHgvRHLLLVSRRgpdapgAAELVAELAALGAEVTVAACDVADRAALAALLAAVPADHP 274

                        90
                ....*....|.
gi 32445327  88 IAGLVHSAGSL 98
Cdd:cd08956 275 LTAVVHAAGVL 285
PRK07856 PRK07856
SDR family oxidoreductase;
18-96 4.96e-06

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 46.47  E-value: 4.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVEllqslSEACGSRVTTVAADLCSIAGVEQLLASIPSDS-EIAGLVHSAG 96
Cdd:PRK07856  10 LVTGGTRGIGAGIARAFLAAGATVVVCGRRAP-----ETVDGRPAEFHAADVRDPDQVAALVDAIVERHgRLDVLVNNAG 84
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 18-96 4.96e-06

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 46.54  E-value: 4.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFR-VFAVGRSVE---LLQSLSEACGSRVTTVAADLCSIAGVEQLLA-SIPSDSEIAGLV 92
Cdd:PRK06198  10 LVTGGTQGLGAAIARAFAERGAAgLVICGRNAEkgeAQAAELEALGAKAVFVQADLSDVEDCRRVVAaADEAFGRLDALV 89


                 ....
gi 32445327   93 HSAG 96
Cdd:PRK06198  90 NAAG 93
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 16-230 5.22e-06

meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases (BDHs) catalyze the NAD+ dependent conversion of 2,3-butanediol to acetonin; BDHs are classified into types according to their stereospecificity as to substrates and products. Included in this subgroup are Klebsiella pneumonia meso-BDH which catalyzes meso-2,3-butanediol to D(-)-acetonin, and Corynebacterium glutamicum L-BDH which catalyzes lX+)-2,3-butanediol to L(+)-acetonin. This subgroup is comprised of classical SDRs with the characteristic catalytic triad and NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 46.60  E-value: 5.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVE-----LLQSLSEAcGSRVTTVAADLCSIAGVEQLLASIPSD-SEIA 89
Cdd:cd05366   4 VAIITGAAQGIGRAIAERLAADGFNIVLADLNLEeaaksTIQEISEA-GYNAVAVGADVTDKDDVEALIDQAVEKfGSFD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  90 GLVHSAGsLVPLQPYEQIDMNELAEHFRIHV-GV------PIELFNSLSRDctvKRMLFIDSYSASNARLGWGAYSIVKA 162
Cdd:cd05366  83 VMVNNAG-IAPITPLLTITEEDLKKVYAVNVfGVlfgiqaAARQFKKLGHG---GKIINASSIAGVQGFPNLGAYSASKF 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32445327 163 AAQMAARCAAQEL-PGTRTIRAY-PGAVNTRIVDAVLASDTQTA--------STFASMREKGEFAEPEDVARfLVALL 230
Cdd:cd05366 159 AVRGLTQTAAQELaPKGITVNAYaPGIVKTEMWDYIDEEVGEIAgkpegegfAEFSSSIPLGRLSEPEDVAG-LVSFL 235
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 18-68 6.36e-06

insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 46.14  E-value: 6.36e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRS--VELLQSLSEACGS-RVTTVAAD 68
Cdd:cd05323   4 IITGGASGIGLATAKLLLKKGAKVAILDRNenPGAAAELQAINPKvKATFVQCD 57
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 24-233 6.65e-06

Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 45.88  E-value: 6.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327    24 RGIGRAVAKELAGRGFRVFAVGRSVEL---LQSLSEACGSRVttVAADLCSIAGVEQLLASIPSD-SEIAGLVHSAGSLV 99
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALakrVEELAEELGAAV--LPCDVTDEEQVEALVAAAVEKfGRLDILVNNAGFAP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   100 PLQ-PYEQIDMNELAEHFRIHVgvpielfNSLSRDC-TVKRML-------FIDSYSASNARLGWGAYSIVKAAAQMAARC 170
Cdd:pfam13561  84 KLKgPFLDTSREDFDRALDVNL-------YSLFLLAkAALPLMkeggsivNLSSIGAERVVPNYNAYGAAKAALEALTRY 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32445327   171 AAQELpGTRTIRA---YPGAVNTRIVDAVLASDtqtaSTFASMREK---GEFAEPEDVARFLVALLVDA 233
Cdd:pfam13561 157 LAVEL-GPRGIRVnaiSPGPIKTLAASGIPGFD----ELLAAAEARaplGRLGTPEEVANAAAFLASDL 220
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 19-109 6.80e-06

human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical-SDR subgroup includes the human proteins: type 2 17beta-HSD, type 6 17beta-HSD, type 2 11beta-HSD, dehydrogenase/reductase SDR family member 9, short-chain dehydrogenase/reductase family 9C member 7, 3-hydroxybutyrate dehydrogenase type 1, and retinol dehydrogenase 5. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 46.12  E-value: 6.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  19 VTGATRGIGRAVAKELAGRGFRVFA-----VGRSVELLQslsEACGSRVTTVAADLC---SIAGVEQLLASIPSDSEIAG 90
Cdd:cd09805   5 ITGCDSGFGNLLAKKLDSLGFTVLAgcltkNGPGAKELR---RVCSDRLRTLQLDVTkpeQIKRAAQWVKEHVGEKGLWG 81

                        90
                ....*....|....*....
gi 32445327  91 LVHSAGSLVPLQPYEQIDM 109
Cdd:cd09805  82 LVNNAGILGFGGDEELLPM 100
PRK07063 PRK07063
SDR family oxidoreductase;
18-108 9.70e-06

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 45.81  E-value: 9.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEAC-----GSRVTTVAADLCSIAGVEQLLASipSDSEIAG-- 90
Cdd:PRK07063  11 LVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIardvaGARVLAVPADVTDAASVAAAVAA--AEEAFGPld 88

                         90
                 ....*....|....*....
gi 32445327   91 -LVHSAGSLVPLQPYEQID 108
Cdd:PRK07063  89 vLVNNAGINVFADPLAMTD 107
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
 18-82 1.03e-05

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 45.30  E-value: 1.03e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEAcgsRVTTVAADLCSIAGVEQLLASI 82
Cdd:cd05243   3 LVVGATGKVGRHVVRELLDRGYQVRALVRDPSQAEKLEAA---GAEVVVGDLTDAESLAAALEGI 64
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 16-96 1.03e-05

alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, which catalyzes the NAD-dependent oxidoreduction of hydroxysteroids, is a dimeric member of the classical SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 45.56  E-value: 1.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRsvellqslseacgsRVTTVAADLCSIAGVEQLLASIPSDSE--IAGLVH 93
Cdd:cd05328   1 TIVITGAASGIGAATAELLEDAGHTVIGIDL--------------READVIADLSTPEGRAAAIADVLARCSgvLDGLVN 66


                ...
gi 32445327  94 SAG 96
Cdd:cd05328  67 CAG 69
PRK06139 PRK06139
SDR family oxidoreductase;
18-124 1.06e-05

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 45.87  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSE---ACGSRVTTVAADLCSIAGVEQLLASIPS-DSEIAGLVH 93
Cdd:PRK06139  11 VITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEecrALGAEVLVVPTDVTDADQVKALATQAASfGGRIDVWVN 90

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 32445327   94 SAG-------SLVPLQPYEQIDMNELAEHFR-IHVGVPI 124
Cdd:PRK06139  91 NVGvgavgrfEETPIEAHEQVIQTNLIGYMRdAHAALPI 129
PRK07035 PRK07035
SDR family oxidoreductase;
18-80 1.19e-05

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 45.39  E-value: 1.19e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSE---ACGSRVTTVAadlCSIAGVEQLLA 80
Cdd:PRK07035  12 LVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADaivAAGGKAEALA---CHIGEMEQIDA 74
PRK09730 PRK09730
SDR family oxidoreductase;
18-107 1.20e-05

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 45.23  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVfAVG-----RSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSDSE-IAGL 91
Cdd:PRK09730   5 LVTGGSRGIGRATALLLAQEGYTV-AVNyqqnlHAAQEVVNLITQAGGKAFVLQADISDENQVVAMFTAIDQHDEpLAAL 83

                         90
                 ....*....|....*.
gi 32445327   92 VHSAGSLVPLQPYEQI 107
Cdd:PRK09730  84 VNNAGILFTQCTVENL 99
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 18-261 1.22e-05

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 45.54  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVEllQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLVHSAG 96
Cdd:PRK06463  11 LITGGTRGIGRAIAEAFLREGAKVAVLYNSAE--NEAKELREKGVFTIKCDVGNRDQVKKSKEVVEKEfGRVDVLVNNAG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   97 SLVpLQPYEQIDMNELAEHFRIHVGVPI----ELFNSLSRDctvKRMLFIDsySASNARLGWGA-----YSIVKAAAQMA 167
Cdd:PRK06463  89 IMY-LMPFEEFDEEKYNKMIKINLNGAIyttyEFLPLLKLS---KNGAIVN--IASNAGIGTAAegttfYAITKAGIIIL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  168 ARCAAQELpGTRTIRA---YPGAVNTrivDAVLASDTQTA-----STFASMREKGEFAEPEDVARFLVALLVDATDELIG 239
Cdd:PRK06463 163 TRRLAFEL-GKYGIRVnavAPGWVET---DMTLSGKSQEEaeklrELFRNKTVLKTTGKPEDIANIVLFLASDDARYITG 238

                        250       260
                 ....*....|....*....|..
gi 32445327  240 SRDVFDynnpGDRADvfQLTRS 261
Cdd:PRK06463 239 QVIVAD----GGRID--NLTHS 254
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 19-92 1.27e-05

classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187608 [Multi-domain]  Cd Length: 239  Bit Score: 45.01  E-value: 1.27e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32445327  19 VTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPS-DSEIAGLV 92
Cdd:cd05350   3 ITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNPSVEVEILDVTDEERNQLVIAElEAELGGLD 77
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 18-96 1.29e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 45.28  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVellqslSEACGSRVTTVAADLCSIAGVEQLLASIpsdSEIAG----LVH 93
Cdd:PRK06523  13 LVTGGTKGIGAATVARLLEAGARVVTTARSR------PDDLPEGVEFVAADLTTAEGCAAVARAV---LERLGgvdiLVH 83


                 ...
gi 32445327   94 SAG 96
Cdd:PRK06523  84 VLG 86
PRK05693 PRK05693
SDR family oxidoreductase;
15-190 2.02e-05

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 44.78  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   15 PTYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEAcgsRVTTVAADLCSIAGVEQLLASIpsDSEIAG---L 91
Cdd:PRK05693   2 PVVLITGCSSGIGRALADAFKAAGYEVWATARKAEDVEALAAA---GFTAVQLDVNDGAALARLAEEL--EAEHGGldvL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   92 VHSAGSLVpLQPYEQIDMNELAEHFRIHV----GVPIELFNSLSRdctvKRMLFIDSYSASNARLG--WGAYSIVKAAAQ 165
Cdd:PRK05693  77 INNAGYGA-MGPLLDGGVEAMRRQFETNVfavvGVTRALFPLLRR----SRGLVVNIGSVSGVLVTpfAGAYCASKAAVH 151

                        170       180
                 ....*....|....*....|....*..
gi 32445327  166 MAARCAAQELP--GTRTIRAYPGAVNT 190
Cdd:PRK05693 152 ALSDALRLELApfGVQVMEVQPGAIAS 178
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 16-81 2.22e-05

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 44.70  E-value: 2.22e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFA-VGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLAS 81
Cdd:PRK08642   7 TVLVTGGSRGLGAAIARAFAREGARVVVnYHQSEDAAEALADELGDRAIALQADVTDREQVQAMFAT 73
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 16-236 2.42e-05

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 44.30  E-value: 2.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   16 TYVVTGATR--GIGRAVAKELAGRGFRVF------------AVGRSVE--LLQSLSEACGSRVTTVAADLCSIAGVEQLL 79
Cdd:PRK12748   7 IALVTGASRlnGIGAAVCRRLAAKGIDIFftywspydktmpWGMHDKEpvLLKEEIESYGVRCEHMEIDLSQPYAPNRVF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   80 ASIpsdSEIAG----LVHSAGSLVPlQPYEQIDMNELAEHFRIHVGVPIELFNSLSRDCTVK---RMLFIDSYSASNARL 152
Cdd:PRK12748  87 YAV---SERLGdpsiLINNAAYSTH-TRLEELTAEQLDKHYAVNVRATMLLSSAFAKQYDGKaggRIINLTSGQSLGPMP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  153 GWGAYSIVKAAAQMAARCAAQEL-PGTRTIRAY-PGAVNTRIVDAVLAsdTQTASTFASmrekGEFAEPEDVARfLVALL 230
Cdd:PRK12748 163 DELAYAATKGAIEAFTKSLAPELaEKGITVNAVnPGPTDTGWITEELK--HHLVPKFPQ----GRVGEPVDAAR-LIAFL 235


                 ....*.
gi 32445327  231 vdATDE 236
Cdd:PRK12748 236 --VSEE 239
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 18-240 2.89e-05

rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has bifunctional proteins with an N-terminal aldolase and a C-terminal classical SDR domain. One member is identified as a rhamnulose-1-phosphate aldolase/alcohol dehydrogenase. The SDR domain has a canonical SDR glycine-rich NAD(P) binding motif and a match to the characteristic active site triad. However, it lacks an upstream active site Asn typical of SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 44.31  E-value: 2.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEAC--GSRVTTVAADLCSIAGVEQLLASIPSdsEIAGL---V 92
Cdd:cd08943   5 LVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAqgGPRALGVQCDVTSEAQVQSAFEQAVL--EFGGLdivV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  93 HSAGsLVPLQPYEQIDMNELAEHFRI----HVGVPIELFNSLSRDCTVKRMLFIDSYSASNARLGWGAYSIVKAAAQMAA 168
Cdd:cd08943  83 SNAG-IATSSPIAETSLEDWNRSMDInltgHFLVSREAFRIMKSQGIGGNIVFNASKNAVAPGPNAAAYSAAKAAEAHLA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327 169 RCAAQELpGTRTIRaypgaVNTRIVDAVL--ASDTQTASTFASMREKGEFAE-------------PEDVARFLVALLVDA 233
Cdd:cd08943 162 RCLALEG-GEDGIR-----VNTVNPDAVFrgSKIWEGVWRAARAKAYGLLEEeyrtrnllkrevlPEDVAEAVVAMASED 235


                ....*..
gi 32445327 234 TDELIGS 240
Cdd:cd08943 236 FGKTTGA 242
PRK07024 PRK07024
SDR family oxidoreductase;
18-73 2.98e-05

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 44.15  E-value: 2.98e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACG--SRVTTVAADLCSIA 73
Cdd:PRK07024   6 FITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPkaARVSVYAADVRDAD 63
PRK06124 PRK06124
SDR family oxidoreductase;
16-161 3.17e-05

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 43.93  E-value: 3.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSE---ACGSRVTTVAADLCSIAGVEQLLASI-PSDSEIAGL 91
Cdd:PRK06124  13 VALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAalrAAGGAAEALAFDIADEEAVAAAFARIdAEHGRLDIL 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32445327   92 VHSAGSLvPLQPYEQIDMNELAEHFRIHVGVPIelfnSLSRDCTVK-------RMLFIDSYSASNARLGWGAYSIVK 161
Cdd:PRK06124  93 VNNVGAR-DRRPLAELDDAAIRALLETDLVAPI----LLSRLAAQRmkrqgygRIIAITSIAGQVARAGDAVYPAAK 164
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 16-246 3.23e-05

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 44.12  E-value: 3.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSE---ACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGL 91
Cdd:PRK13394   9 TAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADeinKAGGKAIGVAMDVTNEDAVNAGIDKVAERfGSVDIL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   92 VHSAGSLVpLQPYEQIDMNELAEHFRIHVGVPI----ELFNSLSRDCTVKRMLFIDSYSASNARLGWGAYSIVKAAAQMA 167
Cdd:PRK13394  89 VSNAGIQI-VNPIENYSFADWKKMQAIHVDGAFlttkAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGL 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  168 ARCAAQELPGTRtIRAY---PGAVNTRIVDAVLasDTQTASTFASMRE-----------KGEFAEPEDVARFLVALLVDA 233
Cdd:PRK13394 168 ARVLAKEGAKHN-VRSHvvcPGFVRTPLVDKQI--PEQAKELGISEEEvvkkvmlgktvDGVFTTVEDVAQTVLFLSSFP 244

                        250
                 ....*....|...
gi 32445327  234 TDELIGSRDVFDY 246
Cdd:PRK13394 245 SAALTGQSFVVSH 257
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 19-231 3.44e-05

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 43.94  E-value: 3.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   19 VTGATRGIGRAVAKELAGRGFRVFAVG----RSVELLQ---SLSEACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAG 90
Cdd:PRK12827  11 ITGGSGGLGRAIAVRLAADGADVIVLDihpmRGRAEADavaAGIEAAGGKALGLAFDVRDFAATRAALDAGVEEfGRLDI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   91 LVHSAGsLVPLQPYEQIDMNELAEHFRI------HVGVPieLFNSLSRDCTVKRMLFIDSYSASNARLGWGAYSIVKAAA 164
Cdd:PRK12827  91 LVNNAG-IATDAAFAELSIEEWDDVIDVnldgffNVTQA--ALPPMIRARRGGRIVNIASVAGVRGNRGQVNYAASKAGL 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  165 QMAARCAAQELpGTRTIRA---YPGAVNTRIVDAVLASDTQTASTFASMRekgefAEPEDVARfLVALLV 231
Cdd:PRK12827 168 IGLTKTLANEL-APRGITVnavAPGAINTPMADNAAPTEHLLNPVPVQRL-----GEPDEVAA-LVAFLV 230
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 18-245 3.64e-05

3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187600 [Multi-domain]  Cd Length: 247  Bit Score: 43.91  E-value: 3.64e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSDS-EIAGLVHSAG 96
Cdd:cd05341   9 IVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARFFHLDVTDEDGWTAVVDTAREAFgRLDVLVNNAG 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  97 SLVPlQPYEQIDMNELAEHFRIHV-GV------PIELFNSLSRDCTVKrmlfIDSYSASNARLGWGAYSIVKAAAQMAAR 169
Cdd:cd05341  89 ILTG-GTVETTTLEEWRRLLDINLtGVflgtraVIPPMKEAGGGSIIN----MSSIEGLVGDPALAAYNASKGAVRGLTK 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327 170 CAAQEL-PGTRTIRA---YPGAVNTRIVDAVLasDTQTASTFASMREKGEFAEPEDVARFLVALLVDATDELIGSRDVFD 245
Cdd:cd05341 164 SAALECaTQGYGIRVnsvHPGYIYTPMTDELL--IAQGEMGNYPNTPMGRAGEPDEIAYAVVYLASDESSFVTGSELVVD 241
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 19-192 3.82e-05

daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Daunorubicin C-13 ketoreductase is member of the classical SDR family with a canonical glycine-rich NAD(P)-binding motif, but lacking a complete match to the active site tetrad characteristic of this group. The critical Tyr, plus the Lys and upstream Asn are present, but the catalytic Ser is replaced, generally by Gln. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 44.02  E-value: 3.82e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  19 VTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSDSEIAGLVHSAGSL 98
Cdd:cd08951  12 ITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLIGDLSSLAETRKLADQVNAIGRFDAVIHNAGIL 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  99 vpLQPYEQIDMNELAEHFRIHVGVPIELFNSLSRDctvKRMLFIDS--YSASNARL--------GWG---AYSIVKAAAQ 165
Cdd:cd08951  92 --SGPNRKTPDTGIPAMVAVNVLAPYVLTALIRRP---KRLIYLSSgmHRGGNASLddidwfnrGENdspAYSDSKLHVL 166

                       170       180
                ....*....|....*....|....*..
gi 32445327 166 MAARCAAQELPGTRTIRAYPGAVNTRI 192
Cdd:cd08951 167 TLAAAVARRWKDVSSNAVHPGWVPTKM 193
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 15-95 3.94e-05

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 43.90  E-value: 3.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   15 PTYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLS---EACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAG 90
Cdd:PRK07677   2 KVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKleiEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKfGRIDA 81


                 ....*
gi 32445327   91 LVHSA 95
Cdd:PRK07677  82 LINNA 86
PRK09186 PRK09186
flagellin modification protein A; Provisional
 16-121 3.96e-05

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 43.83  E-value: 3.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFA----VGRSVELLQSLSEACGSRVTTVAA-DLCSIAGVEQLLASIPSD-SEIA 89
Cdd:PRK09186   6 TILITGAGGLIGSALVKAILEAGGIVIAadidKEALNELLESLGKEFKSKKLSLVElDITDQESLEEFLSKSAEKyGKID 85

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 32445327   90 GLVHSA-------GSLvplqpYEQIDMNELAEHFRIHVG 121
Cdd:PRK09186  86 GAVNCAyprnkdyGKK-----FFDVSLDDFNENLSLHLG 119
SDR_a3 cd05229
atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a ...
 19-69 4.38e-05

atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a glycine-rich NAD(P)-binding motif consensus that is very similar to the extended SDRs, GXXGXXG. Generally, this group has poor conservation of the active site tetrad, However, individual sequences do contain matches to the YXXXK active site motif, and generally Tyr or Asn in place of the upstream Ser found in most SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187540 [Multi-domain]  Cd Length: 302  Bit Score: 43.86  E-value: 4.38e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 32445327  19 VTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEacgsrVTTVAADL 69
Cdd:cd05229   4 VLGASGPIGREVARELRRRGWDVRLVSRSGSKLAWLPG-----VEIVAADA 49
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 16-239 4.51e-05

glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR family, it catalyzes the NAD(P)-dependent oxidation of beta-D-glucose to D-glucono-delta-lactone. GlcDH has a typical NAD-binding site glycine-rich pattern as well as the canonical active site tetrad (YXXXK motif plus upstream Ser and Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187616 [Multi-domain]  Cd Length: 253  Bit Score: 43.53  E-value: 4.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRS----VELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIpsDSEIAG- 90
Cdd:cd05358   5 VALVTGASSGIGKAIAIRLATAGANVVVNYRSkedaAEEVVEEIKAVGGKAIAVQADVSKEEDVVALFQSA--IKEFGTl 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  91 --LVHSAGslvpLQ-PYEQIDMNelAEHFRIHVGVPIELFNSLSRDcTVKRMLF------IDSYSASNARLGWG---AYS 158
Cdd:cd05358  83 diLVNNAG----LQgDASSHEMT--LEDWNKVIDVNLTGQFLCARE-AIKRFRKskikgkIINMSSVHEKIPWPghvNYA 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327 159 IVKAAAQMAARCAAQELpGTRTIRAY---PGAVNTRIVDAVLASDTQTASTFaSMREKGEFAEPEDVARFLVALLVDATD 235
Cdd:cd05358 156 ASKGGVKMMTKTLAQEY-APKGIRVNaiaPGAINTPINAEAWDDPEQRADLL-SLIPMGRIGEPEEIAAAAAWLASDEAS 233


                ....
gi 32445327 236 ELIG 239
Cdd:cd05358 234 YVTG 237
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
18-223 5.36e-05

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 43.56  E-value: 5.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSE---ACGSRVTTVAADlcsIAGVEQLLASIPSDSEIAG---- 90
Cdd:PRK08643   6 LVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADklsKDGGKAIAVKAD---VSDRDQVFAAVRQVVDTFGdlnv 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   91 LVHSAGsLVPLQPYEQIDMNELAEHFRIHVG-------VPIELFNSLSRDCTVkrmlfIDSYSAS----NARLgwGAYSI 159
Cdd:PRK08643  83 VVNNAG-VAPTTPIETITEEQFDKVYNINVGgviwgiqAAQEAFKKLGHGGKI-----INATSQAgvvgNPEL--AVYSS 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32445327  160 VKAAAQMAARCAAQEL-PGTRTIRAY-PGAVNTRIVDAVLASDTQTA--------STFASMREKGEFAEPEDVA 223
Cdd:PRK08643 155 TKFAVRGLTQTAARDLaSEGITVNAYaPGIVKTPMMFDIAHQVGENAgkpdewgmEQFAKDITLGRLSEPEDVA 228
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 18-238 5.58e-05

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 43.24  E-value: 5.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATR--GIGRAVAKELAGRGFRVF-----AVGRSVE---------LLQSLSEACGSRVTTVAADLCSIAGVEQLLAS 81
Cdd:PRK12859  10 VVTGVSRldGIGAAICKELAEAGADIFftywtAYDKEMPwgvdqdeqiQLQEELLKNGVKVSSMELDLTQNDAPKELLNK 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   82 IpsdSEIAG----LVHSAGSLVPLqPYEQIDMNELAEHFRIHVGVPIELFNSLSRDCTVK---RMLFIDSYSASNARLGW 154
Cdd:PRK12859  90 V---TEQLGyphiLVNNAAYSTNN-DFSNLTAEELDKHYMVNVRATTLLSSQFARGFDKKsggRIINMTSGQFQGPMVGE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  155 GAYSIVKAAAQMAARCAAQELPGTR-TIRAY-PGAVNTRIVDAVLASDTQTASTFasmrekGEFAEPEDVARfLVALLVD 232
Cdd:PRK12859 166 LAYAATKGAIDALTSSLAAEVAHLGiTVNAInPGPTDTGWMTEEIKQGLLPMFPF------GRIGEPKDAAR-LIKFLAS 238


                 ....*.
gi 32445327  233 ATDELI 238
Cdd:PRK12859 239 EEAEWI 244
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 17-107 5.66e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 43.47  E-value: 5.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   17 YVVTGATrGIGRAVAKELaGRGFRVFAVGRSVELLQS----LSEAcGSRVTTVAADLCSIAGVEQLLASIPSDSEIAGLV 92
Cdd:PRK06940   5 VVVIGAG-GIGQAIARRV-GAGKKVLLADYNEENLEAaaktLREA-GFDVSTQEVDVSSRESVKALAATAQTLGPVTGLV 81

                         90
                 ....*....|....*.
gi 32445327   93 HSAGsLVPLQ-PYEQI 107
Cdd:PRK06940  82 HTAG-VSPSQaSPEAI 96
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
18-161 6.32e-05

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 44.07  E-value: 6.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGS--RVTTVAADLCSIAGVEQLLAsipsdsEIAG----- 90
Cdd:PRK08324 426 LVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGpdRALGVACDVTDEAAVQAAFE------EAALafggv 499

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32445327   91 --LVHSAGsLVPLQPYEQIDMNELAEHFRI----HVGVPIELFNSLSRDCTVKRMLFIDSYSASNARLGWGAYSIVK 161
Cdd:PRK08324 500 diVVSNAG-IAISGPIEETSDEDWRRSFDVnatgHFLVAREAVRIMKAQGLGGSIVFIASKNAVNPGPNFGAYGAAK 575
PRK05993 PRK05993
SDR family oxidoreductase;
11-80 6.63e-05

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 43.09  E-value: 6.63e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32445327   11 MQAIPTYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLsEACGsrVTTVAADLC---SIA-GVEQLLA 80
Cdd:PRK05993   1 MDMKRSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAAL-EAEG--LEAFQLDYAepeSIAaLVAQVLE 71
MupV_like_SDR_e cd05263
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ...
 17-98 6.81e-05

Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family domains have the characteristic active site tetrad and a well-conserved NAD(P)-binding motif. This subgroup is not well characterized, its members are annotated as having a variety of putative functions. One characterized member is Pseudomonas fluorescens MupV a protein involved in the biosynthesis of Mupirocin, a polyketide-derived antibiotic. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187573 [Multi-domain]  Cd Length: 293  Bit Score: 43.12  E-value: 6.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  17 YVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEAC-----GSRVTTVAADLCSIAGVEQLLASIPSDSEIAGL 91
Cdd:cd05263   1 VFVTGGTGFLGRHLVKRLLENGFKVLVLVRSESLGEAHERIEeagleADRVRVLEGDLTQPNLGLSAAASRELAGKVDHV 80


                ....*..
gi 32445327  92 VHSAGSL 98
Cdd:cd05263  81 IHCAASY 87
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 18-100 6.90e-05

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 43.22  E-value: 6.90e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLS---EACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLVH 93
Cdd:cd08935   9 VITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAkeiTALGGRAIALAADVLDRASLERAREEIVAQfGTVDILIN 88


                ....*..
gi 32445327  94 SAGSLVP 100
Cdd:cd08935  89 GAGGNHP 95
PRK06123 PRK06123
SDR family oxidoreductase;
18-120 8.57e-05

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 42.84  E-value: 8.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRV----FAVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIpsDSE---IAG 90
Cdd:PRK06123   6 IITGASRGIGAATALLAAERGYAVclnyLRNRDAAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAV--DRElgrLDA 83

                         90       100       110
                 ....*....|....*....|....*....|
gi 32445327   91 LVHSAGSLVPLQPYEQIDMNELAEHFRIHV 120
Cdd:PRK06123  84 LVNNAGILEAQMRLEQMDAARLTRIFATNV 113
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 18-245 9.11e-05

classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site tetrad and glycine-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187648 [Multi-domain]  Cd Length: 246  Bit Score: 42.86  E-value: 9.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASipSDSEIAG---LVHS 94
Cdd:cd08944   7 IVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQQVAALFER--AVEEFGGldlLVNN 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  95 AGSLVPLQPYEQIDMNELAEHFRIHV-GVPIELFNSLSRdcTVKR----MLFIDSYSASNARLGWGAYSIVKAAAQMAAR 169
Cdd:cd08944  85 AGAMHLTPAIIDTDLAVWDQTMAINLrGTFLCCRHAAPR--MIARgggsIVNLSSIAGQSGDPGYGAYGASKAAIRNLTR 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327 170 CAAQELpGTRTIRA---YPGAVNTRIVDAVLASDTQT--ASTFASMREK--GEFAEPEDVARFLVALLVDATDELIGSRD 242
Cdd:cd08944 163 TLAAEL-RHAGIRCnalAPGLIDTPLLLAKLAGFEGAlgPGGFHLLIHQlqGRLGRPEDVAAAVVFLLSDDASFITGQVL 241


                ...
gi 32445327 243 VFD 245
Cdd:cd08944 242 CVD 244
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 16-232 9.23e-05

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 42.44  E-value: 9.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGS--RVTTVAADLCSIAGVEQLLASIPS-DSEIAGLV 92
Cdd:PRK05786   7 KVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKygNIHYVVGDVSSTESARNVIEKAAKvLNAIDGLV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   93 HSAGSLVPlQPYEqiDMNELAEHFRIHVGVPIELFNS----LSRDCTVkrmLFIDS----YSASNARLgwgAYSIVKAAA 164
Cdd:PRK05786  87 VTVGGYVE-DTVE--EFSGLEEMLTNHIKIPLYAVNAslrfLKEGSSI---VLVSSmsgiYKASPDQL---SYAVAKAGL 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32445327  165 QMAARCAAQELPGtRTIRaypgaVNTrIVDAVLASDTQTASTFASMREKGEF-AEPEDVARFLVALLVD 232
Cdd:PRK05786 158 AKAVEILASELLG-RGIR-----VNG-IAPTTISGDFEPERNWKKLRKLGDDmAPPEDFAKVIIWLLTD 219
PRK08177 PRK08177
SDR family oxidoreductase;
16-126 1.09e-04

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 42.32  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVaaDLCSIAGVEQLLASIpSDSEIAGLVHSA 95
Cdd:PRK08177   3 TALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTALQALPGVHIEKL--DMNDPASLDQLLQRL-QGQRFDLLFVNA 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 32445327   96 GSLVPL-QPYEQIDMNELAEHFRIHVGVPIEL 126
Cdd:PRK08177  80 GISGPAhQSAADATAAEIGQLFLTNAIAPIRL 111
PRK06500 PRK06500
SDR family oxidoreductase;
19-245 1.09e-04

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 42.64  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   19 VTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLVHSAGS 97
Cdd:PRK06500  11 ITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGESALVIRADAGDVAAQKALAQALAEAfGRLDAVFINAGV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   98 lVPLQPYEQIDMNELAEHFRIHVGVPIELFNSLsrdctvkrmLFIDSYSAS-------NARLGW---GAYSIVKAAAQMA 167
Cdd:PRK06500  91 -AKFAPLEDWDEAMFDRSFNTNVKGPYFLIQAL---------LPLLANPASivlngsiNAHIGMpnsSVYAASKAALLSL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  168 ARCAAQELPGtRTIRA---YPGAVNTRIVDAVLASDTQTASTFASMREK---GEFAEPEDVARFLVALLVDATDELIGSR 241
Cdd:PRK06500 161 AKTLSGELLP-RGIRVnavSPGPVQTPLYGKLGLPEATLDAVAAQIQALvplGRFGTPEEIAKAVLYLASDESAFIVGSE 239


                 ....
gi 32445327  242 DVFD 245
Cdd:PRK06500 240 IIVD 243
NmrA pfam05368
NmrA-like family; NmrA is a negative transcriptional regulator involved in the ...
 18-80 1.10e-04

NmrA-like family; NmrA is a negative transcriptional regulator involved in the post-translational modification of the transcription factor AreA. NmrA is part of a system controlling nitrogen metabolite repression in fungi. This family only contains a few sequences as iteration results in significant matches to other Rossmann fold families.


Pssm-ID: 398829 [Multi-domain]  Cd Length: 236  Bit Score: 42.33  E-value: 1.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32445327    18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSV--ELLQSLSEAcgsRVTTVAADLCSIAGVEQLLA 80
Cdd:pfam05368   2 LVFGATGQQGGSVVRASLKAGHKVRALVRDPksELAKSLKEA---GVELVKGDLDDKESLVEALK 63
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 18-122 1.19e-04

human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are classical SDRs, with a canonical active site tetrad and a close match to the typical Gly-rich NAD-binding motif. Human DHRS6 is a cytosolic type 2 (R)-hydroxybutyrate dehydrogenase, which catalyses the conversion of (R)-hydroxybutyrate to acetoacetate. Also included in this subgroup is Escherichia coli UcpA (upstream cys P). Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. Note: removed : needed to make this chiodl smaller when drew final trees: rmeoved text form description: Other proteins in this subgroup include Thermoplasma acidophilum aldohexose dehydrogenase, which has high dehydrogenase activity against D-mannose, Bacillus subtilis BacC involved in the biosynthesis of the dipeptide bacilysin and its antibiotic moiety anticapsin, Sphingomonas paucimobilis strain B90 LinC, involved in the degradation of hexachlorocyclohexane isomers...... P).


Pssm-ID: 187626 [Multi-domain]  Cd Length: 241  Bit Score: 42.46  E-value: 1.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLseACGSRVTTVAADLCSIAGVEQLLASIPSDS---EIAGLVHS 94
Cdd:cd05368   6 LITAAAQGIGRAIALAFAREGANVIATDINEEKLKEL--ERGPGITTRVLDVTDKEQVAALAKEEGRIDvlfNCAGFVHH 83

                        90       100
                ....*....|....*....|....*...
gi 32445327  95 AGSLvplqpyeqiDMNELAEHFRIHVGV 122
Cdd:cd05368  84 GSIL---------DCEDDDWDFAMNLNV 102
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 16-82 1.23e-04

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR; This subgroup includes Rhizobium sp. NGR234 FabG1. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 42.44  E-value: 1.23e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRGFRVfAVG--RSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASI 82
Cdd:cd05349   2 VVLVTGASRGLGAAIARSFAREGARV-VVNyyRSTESAEAVAAEAGERAIAIQADVRDRDQVQAMIEEA 69
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 18-96 1.31e-04

3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 42.21  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSDSE-IAGLVHSAG 96
Cdd:PRK12936  10 LVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGERVKIFPANLSDRDEVKALGQKAEADLEgVDILVNNAG 89
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 18-82 1.58e-04

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 41.97  E-value: 1.58e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSL-SEACGSRVTTVAADLCSIAGVEQLLASI 82
Cdd:PRK12829  15 LVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATaARLPGAKVTATVADVADPAQVERVFDTA 80
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 15-49 1.79e-04

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human DHRS1 and human HSDL2 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 41.61  E-value: 1.79e-04
                        10        20        30
                ....*....|....*....|....*....|....*
gi 32445327  15 PTYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVE 49
Cdd:cd05338   4 KVAFVTGASRGIGRAIALRLAKAGATVVVAAKTAS 38
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 18-80 1.92e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 41.84  E-value: 1.92e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSE---ACGSRVTTVAADLCSIAGVEQLLA 80
Cdd:PRK07478  10 IITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAeirAEGGEAVALAGDVRDEAYAKALVA 75
NmrA_TMR_like_1_SDR_a cd05231
NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, ...
 17-80 1.92e-04

NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, subgroup 1, atypical (a) SDRs; Atypical SDRs related to NMRa, TMR, and HSCARG (an NADPH sensor). This subgroup resembles the SDRs and has a partially conserved characteristic [ST]GXXGXXG NAD-binding motif, but lacks the conserved active site residues. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Atypical SDRs are distinct from classical SDRs. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187542 [Multi-domain]  Cd Length: 259  Bit Score: 41.93  E-value: 1.92e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32445327  17 YVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEAcGSRVttVAADLCSIAGVEQLLA 80
Cdd:cd05231   1 ILVTGATGRIGSKVATTLLEAGRPVRALVRSDERAAALAAR-GAEV--VVGDLDDPAVLAAALA 61
PRK09135 PRK09135
pteridine reductase; Provisional
 10-100 2.34e-04

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 41.45  E-value: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   10 NMQAIPTYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVE-----LLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPS 84
Cdd:PRK09135   2 MTDSAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRSAaeadaLAAELNALRPGSAAALQADLLDPDALPELVAACVA 81

                         90
                 ....*....|....*..
gi 32445327   85 D-SEIAGLVHSAGSLVP 100
Cdd:PRK09135  82 AfGRLDALVNNASSFYP 98
PLN02896 PLN02896
cinnamyl-alcohol dehydrogenase
 13-151 2.41e-04

cinnamyl-alcohol dehydrogenase


Pssm-ID: 178484 [Multi-domain]  Cd Length: 353  Bit Score: 41.73  E-value: 2.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   13 AIPTYVVTGATRGIGRAVAKELAGRGFRVFAVGR----SVELLQSLSEacGSRVTTVAADLCSIAGVEQLLASipsdseI 88
Cdd:PLN02896   9 ATGTYCVTGATGYIGSWLVKLLLQRGYTVHATLRdpakSLHLLSKWKE--GDRLRLFRADLQEEGSFDEAVKG------C 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32445327   89 AGLVHSAGSlvpLQPYEQIDMNELAEHFRIHVGVP-----IELFNSLSRDCTVKRMLFIDSYSASNAR 151
Cdd:PLN02896  81 DGVFHVAAS---MEFDVSSDHNNIEEYVQSKVIDPaikgtLNVLKSCLKSKTVKRVVFTSSISTLTAK 145
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
 19-77 2.41e-04

Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 40.85  E-value: 2.41e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32445327  19 VTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQ 77
Cdd:cd05226   3 ILGATGFIGRALARELLEQGHEVTLLVRNTKRLSKEDQEPVAVVEGDLRDLDSLSDAVQ 61
COG5322 COG5322
Predicted amino acid dehydrogenase [General function prediction only];
16-56 2.67e-04

Predicted amino acid dehydrogenase [General function prediction only];


Pssm-ID: 444114 [Multi-domain]  Cd Length: 362  Bit Score: 41.75  E-value: 2.67e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSE 56
Cdd:COG5322 153 TVAVVGATGSIGSVCARLLAREVKRLTLVARNLERLEELAE 193
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 18-96 2.76e-04

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 41.75  E-value: 2.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFA--VGRSVELLQSLSEACGSrvTTVAADLCSIAGVEQLLASIPS-DSEIAGLVHS 94
Cdd:PRK08261 214 LVTGAARGIGAAIAEVLARDGAHVVCldVPAAGEALAAVANRVGG--TALALDITAPDAPARIAEHLAErHGGLDIVVHN 291


                 ..
gi 32445327   95 AG 96
Cdd:PRK08261 292 AG 293
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 16-101 3.72e-04

classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an incomplete match to the canonical glycine rich NAD-binding motif and lacks the typical active site tetrad (instead of the critical active site Tyr, it has Phe, but contains the nearby Lys). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 40.83  E-value: 3.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVE----LLQSLSEACGSRVTTVAADLCSIAGVEQLLASIpsDSEIAG- 90
Cdd:cd05373   1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAkleaLLVDIIRDAGGSAKAVPTDARDEDEVIALFDLI--EEEIGPl 78

                        90
                ....*....|...
gi 32445327  91 --LVHSAGSLVPL 101
Cdd:cd05373  79 evLVYNAGANVWF 91
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
16-110 3.75e-04

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 40.87  E-value: 3.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFAV--GRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLV 92
Cdd:PRK06935  17 VAIVTGGNTGLGQGYAVALAKAGADIIITthGTNWDETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEfGKIDILV 96

                         90       100
                 ....*....|....*....|
gi 32445327   93 HSAGSL--VPLQPYEQIDMN 110
Cdd:PRK06935  97 NNAGTIrrAPLLEYKDEDWN 116
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 18-85 3.84e-04

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 41.14  E-value: 3.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQS-------------LSEACGSRVTTVAADLCSIAGVEQLLASIPS 84
Cdd:PRK08303  12 LVAGATRGAGRGIAVELGAAGATVYVTGRSTRARRSeydrpetieetaeLVTAAGGRGIAVQVDHLVPEQVRALVERIDR 91


                 .
gi 32445327   85 D 85
Cdd:PRK08303  92 E 92
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 18-82 4.55e-04

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 40.65  E-value: 4.55e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSE---ACGSRVTTVAADLCSIAGVEQLLASI 82
Cdd:PRK08277  14 VITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAeikAAGGEALAVKADVLDKESLEQARQQI 81
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 16-97 4.69e-04

RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is an SDR-family beta-ketoacyl reductase involved in Rhamnolipid biosynthesis. RhlG is similar to but distinct from the FabG family of beta-ketoacyl-acyl carrier protein (ACP) of type II fatty acid synthesis. RhlG and related proteins are classical SDRs, with a canonical active site tetrad and glycine-rich NAD(P)-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187646 [Multi-domain]  Cd Length: 250  Bit Score: 40.54  E-value: 4.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVA--ADLCSIAGVEQLLASIPSDSE-IAGLV 92
Cdd:cd08942   8 IVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAYGECIAipADLSSEEGIEALVARVAERSDrLDVLV 87


                ....*
gi 32445327  93 HSAGS 97
Cdd:cd08942  88 NNAGA 92
PRK06482 PRK06482
SDR family oxidoreductase;
16-75 5.66e-04

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 40.48  E-value: 5.66e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVAADLCSIAGV 75
Cdd:PRK06482   4 TWFITGASSGFGRGMTERLLARGDRVAATVRRPDALDDLKARYGDRLWVLQLDVTDSAAV 63
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
18-103 5.76e-04

enoyl-[acyl-carrier-protein] reductase FabL;


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 40.47  E-value: 5.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAV-GRSVELLQSLS---EACGSRVTTVAADLCSIAGVEQLLASIpsDSEIAGL-- 91
Cdd:PRK08063   8 LVTGSSRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAeeiEALGRKALAVKANVGDVEKIKEMFAQI--DEEFGRLdv 85

                         90
                 ....*....|...
gi 32445327   92 -VHSAGSLVpLQP 103
Cdd:PRK08063  86 fVNNAASGV-LRP 97
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 16-233 6.60e-04

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187610 [Multi-domain]  Cd Length: 252  Bit Score: 40.01  E-value: 6.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRS----VELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAG 90
Cdd:cd05352  10 VAIVTGGSRGIGLAIARALAEAGADVAIIYNSapraEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQKDfGKIDI 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  91 LVHSAGSLVPL----QPYEQ----IDMNELAEHFRIHVGVPI---ELFNSLsrdctvkrmLFIDSYSAS--NARLGWGAY 157
Cdd:cd05352  90 LIANAGITVHKpaldYTYEQwnkvIDVNLNGVFNCAQAAAKIfkkQGKGSL---------IITASMSGTivNRPQPQAAY 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32445327 158 SIVKAAAQMAARCAAQEL--PGTRTIRAYPGAVNTRIVDAVlasDTQTASTFASMREKGEFAEPEDVARFLVALLVDA 233
Cdd:cd05352 161 NASKAAVIHLAKSLAVEWakYFIRVNSISPGYIDTDLTDFV---DKELRKKWESYIPLKRIALPEELVGAYLYLASDA 235
PRK08017 PRK08017
SDR family oxidoreductase;
11-116 7.16e-04

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 40.07  E-value: 7.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   11 MQAipTYVVTGATRGIGRAVAKELAGRGFRVFAVGR---SVELLQSLSeacgsrVTTVAADLCSIAGVEQLLASIP--SD 85
Cdd:PRK08017   1 MQK--SVLITGCSSGIGLEAALELKRRGYRVLAACRkpdDVARMNSLG------FTGILLDLDDPESVERAADEVIalTD 72

                         90       100       110
                 ....*....|....*....|....*....|.
gi 32445327   86 SEIAGLVHSAGSLVpLQPYEQIDMNELAEHF 116
Cdd:PRK08017  73 NRLYGLFNNAGFGV-YGPLSTISRQQMEQQF 102
PRK12746 PRK12746
SDR family oxidoreductase;
18-96 7.63e-04

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 40.02  E-value: 7.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRV-FAVGRSV----ELLQSLsEACGSRVTTVAADLCSIAGVEQLLASIPSD------- 85
Cdd:PRK12746  10 LVTGASRGIGRAIAMRLANDGALVaIHYGRNKqaadETIREI-ESNGGKAFLIEADLNSIDGVKKLVEQLKNElqirvgt 88

                         90
                 ....*....|.
gi 32445327   86 SEIAGLVHSAG 96
Cdd:PRK12746  89 SEIDILVNNAG 99
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 18-45 7.66e-04

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 39.92  E-value: 7.66e-04
                         10        20
                 ....*....|....*....|....*...
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVfAVG 45
Cdd:PRK07825   9 AITGGARGIGLATARALAALGARV-AIG 35
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 18-96 8.13e-04

human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid dehydrogenases (17betaHSD) are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 17betaHSD type XI, a classical SDR, preferentially converts 3alpha-Adiol to androsterone but not numerous other tested steroids. This subgroup of classical SDRs also includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 39.92  E-value: 8.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGR---SVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLVH 93
Cdd:cd05339   3 LITGGGSGIGRLLALEFAKRGAKVVILDInekGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEvGDVTILIN 82


                ...
gi 32445327  94 SAG 96
Cdd:cd05339  83 NAG 85
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 16-80 9.08e-04

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 39.87  E-value: 9.08e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEA---CGSRVTTVAADLCSIAGVEQLLA 80
Cdd:PRK12429   6 VALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEAlqkAGGKAIGVAMDVTDEEAINAGID 73
PRK07832 PRK07832
SDR family oxidoreductase;
18-67 9.26e-04

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 39.64  E-value: 9.26e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVAA 67
Cdd:PRK07832   4 FVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGTVPE 53
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 18-80 9.48e-04

2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 39.55  E-value: 9.48e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLA 80
Cdd:PRK06200  10 LITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDHVLVVEGDVTSYADNQRAVD 72
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 18-52 1.10e-03

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 39.14  E-value: 1.10e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 32445327  18 VVTGATRGIGRAVAKELAGRGF-RVFAVGRSVELLQ 52
Cdd:cd05324   4 LVTGANRGIGFEIVRQLAKSGPgTVILTARDVERGQ 39
PLN02657 PLN02657
3,8-divinyl protochlorophyllide a 8-vinyl reductase
 16-46 1.18e-03

3,8-divinyl protochlorophyllide a 8-vinyl reductase


Pssm-ID: 178263 [Multi-domain]  Cd Length: 390  Bit Score: 39.75  E-value: 1.18e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGR 46
Cdd:PLN02657  62 TVLVVGATGYIGKFVVRELVRRGYNVVAVAR 92
PRK06953 PRK06953
SDR family oxidoreductase;
15-74 1.19e-03

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 39.28  E-value: 1.19e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32445327   15 PTYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLsEACGSRVTTV-AADLCSIAG 74
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALAAL-QALGAEALALdVADPASVAG 61
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
16-120 1.25e-03

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 39.40  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEAC--GSRVTTVAADlcsIAGVEQLLASIPSDSEIAG--- 90
Cdd:PRK08226   8 TALITGALQGIGEGIARVFARHGANLILLDISPEIEKLADELCgrGHRCTAVVAD---VRDPASVAAAIKRAKEKEGrid 84

                         90       100       110
                 ....*....|....*....|....*....|.
gi 32445327   91 -LVHSAGsLVPLQPYEQIDMNELAEHFRIHV 120
Cdd:PRK08226  85 iLVNNAG-VCRLGSFLDMSDEDRDFHIDINI 114
PRK06194 PRK06194
hypothetical protein; Provisional
 16-78 1.28e-03

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 39.23  E-value: 1.28e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVF-------AVGRSVELLqslsEACGSRVTTVAADLCSIAGVEQL 78
Cdd:PRK06194   8 VAVITGAASGFGLAFARIGAALGMKLVladvqqdALDRAVAEL----RAQGAEVLGVRTDVSDAAQVEAL 73
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 18-100 1.30e-03

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 39.24  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVE-----LLQSLSEACGSRVTTVAADLCSIAGV----EQLLASIPsdsEI 88
Cdd:PRK06197  20 VVTGANTGLGYETAAALAAKGAHVVLAVRNLDkgkaaAARITAATPGADVTLQELDLTSLASVraaaDALRAAYP---RI 96

                         90
                 ....*....|..
gi 32445327   89 AGLVHSAGSLVP 100
Cdd:PRK06197  97 DLLINNAGVMYT 108
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
18-82 1.34e-03

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 39.24  E-value: 1.34e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASI 82
Cdd:PRK07067  10 LLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAA 74
PRK08628 PRK08628
SDR family oxidoreductase;
18-96 1.38e-03

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 39.17  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRS---VELLQSLsEACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLVH 93
Cdd:PRK08628  11 IVTGGASGIGAAISLRLAEEGAIPVIFGRSapdDEFAEEL-RALQPRAEFVQVDLTDDAQCRDAVEQTVAKfGRIDGLVN 89


                 ...
gi 32445327   94 SAG 96
Cdd:PRK08628  90 NAG 92
PRK08340 PRK08340
SDR family oxidoreductase;
18-79 1.66e-03

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 39.02  E-value: 1.66e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGS--RVTTVAADLCSIAGVEQLL 79
Cdd:PRK08340   4 LVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEygEVYAVKADLSDKDDLKNLV 67
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 16-49 1.95e-03

retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup containing retinol-DHs and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 38.60  E-value: 1.95e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVE 49
Cdd:cd09807   3 TVIITGANTGIGKETARELARRGARVIMACRDMA 36
PRK08278 PRK08278
SDR family oxidoreductase;
16-49 2.08e-03

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 38.73  E-value: 2.08e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVE 49
Cdd:PRK08278   8 TLFITGASRGIGLAIALRAARDGANIVIAAKTAE 41
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 15-230 2.28e-03

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 38.55  E-value: 2.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   15 PTYVVTGATRGIGRAVAKELAGRGFRVF--AVGRSVELLQSLSEA--CGSRVTTVAADLCSIAGVEQLL-ASIPSDSEIA 89
Cdd:PRK06077   7 KVVVVTGSGRGIGRAIAVRLAKEGSLVVvnAKKRAEEMNETLKMVkeNGGEGIGVLADVSTREGCETLAkATIDRYGVAD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   90 GLVHSAGsLVPLQPYEQIDMNELAEHFRIHVGVPIELFNSLSRDCT-VKRMLFIDSYSASNARLGWGAYSIVKAAAQMAA 168
Cdd:PRK06077  87 ILVNNAG-LGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEMReGGAIVNIASVAGIRPAYGLSIYGAMKAAVINLT 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32445327  169 RCAAQEL-PGTRTIRAYPGAVNTRIVDAVLASDTQTASTFASMRE-KGEFAEPEDVARFLVALL 230
Cdd:PRK06077 166 KYLALELaPKIRVNAIAPGFVKTKLGESLFKVLGMSEKEFAEKFTlMGKILDPEEVAEFVAAIL 229
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 18-121 2.37e-03

classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad and domain size of the classical SDRs, but has an atypical NAD-binding motif ([ST]G[GA]XGXXG). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187635 [Multi-domain]  Cd Length: 250  Bit Score: 38.47  E-value: 2.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEAC----GSRVTTVAADLCSIAGVEQLLAS-IPSDSEIAGLV 92
Cdd:cd08930   6 LITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELtnlyKNRVIALELDITSKESIKELIESyLEKFGRIDILI 85

                        90       100       110
                ....*....|....*....|....*....|.
gi 32445327  93 HSAG--SLVPLQPYEQIDMNELAEHFRIHVG 121
Cdd:cd08930  86 NNAYpsPKVWGSRFEEFPYEQWNEVLNVNLG 116
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 15-96 2.46e-03

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 38.36  E-value: 2.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   15 PTYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLVH 93
Cdd:PRK06180   5 KTWLITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPDRALARLLDVTDFDAIDAVVADAEATfGPIDVLVN 84


                 ...
gi 32445327   94 SAG 96
Cdd:PRK06180  85 NAG 87
PRK09291 PRK09291
SDR family oxidoreductase;
16-161 2.48e-03

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 38.44  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRS---VELLQSLSEACGSRVTTVAADLCSIAGVEQLLasipsDSEIAGLV 92
Cdd:PRK09291   4 TILITGAGSGFGREVALRLARKGHNVIAGVQIapqVTALRAEAARRGLALRVEKLDLTDAIDRAQAA-----EWDVDVLL 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32445327   93 HSAGSLVPlQPYEQIDMNELAEHFRIHVGVPIELFNSLSRDCTVK---RMLFIDSYSASNARLGWGAYSIVK 161
Cdd:PRK09291  79 NNAGIGEA-GAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARgkgKVVFTSSMAGLITGPFTGAYCASK 149
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 16-82 3.09e-03

Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter sphaeroides SDH, and other SDHs. SDH preferentially interconverts D-sorbitol (D-glucitol) and D-fructose, but also interconverts L-iditol/L-sorbose and galactitol/D-tagatose. SDH is NAD-dependent and is a dimeric member of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 37.98  E-value: 3.09e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASI 82
Cdd:cd05363   5 TALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTDQASIDRCVAAL 71
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 5-65 3.11e-03

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 38.31  E-value: 3.11e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32445327    5 GSWKsnmqaiptyVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTV 65
Cdd:PLN02780  53 GSWA---------LVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYSKT 104
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 16-130 3.19e-03

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 38.02  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSlseacgSRVTTVAADLCSiaGVEQLLASIPSdseIAGLVHSA 95
Cdd:PRK06550   7 TVLITGAASGIGLAQARAFLAQGAQVYGVDKQDKPDLS------GNFHFLQLDLSD--DLEPLFDWVPS---VDILCNTA 75

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 32445327   96 GSLVPLQPYEQIDMNELAEHFRIHVGVPIELFNSL 130
Cdd:PRK06550  76 GILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAY 110
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 18-80 3.30e-03

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 38.10  E-value: 3.30e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLA 80
Cdd:cd05348   8 LITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEGDVRSLADNERAVA 70
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 18-68 4.09e-03

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187627 [Multi-domain]  Cd Length: 249  Bit Score: 37.57  E-value: 4.09e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQS----LSEACGSRVTTVAAD 68
Cdd:cd05369   7 FITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAaaeeISSATGGRAHPIQCD 61
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 16-96 4.23e-03

d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, catalyzes the interconversion of D-3-hydroxybutyrate and acetoacetate. It is a classical SDR, with the canonical NAD-binding motif and active site tetrad. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 37.81  E-value: 4.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRGFRVFAVG-----RSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIpsDSEIAG 90
Cdd:cd08940   4 VALVTGSTSGIGLGIARALAAAGANIVLNGfgdaaEIEAVRAGLAAKHGVKVLYHGADLSKPAAIEDMVAYA--QRQFGG 81


                ....*....
gi 32445327  91 ---LVHSAG 96
Cdd:cd08940  82 vdiLVNNAG 90
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 1-223 5.16e-03

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 37.52  E-value: 5.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327    1 MFLIGSWKSNMQAIptyVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEAC---GSRVTTVAADLCSIAGVEQ 77
Cdd:PRK06113   1 MFNSDNLRLDGKCA---IITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIqqlGGQAFACRCDITSEQELSA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   78 LL-ASIPSDSEIAGLVHSAGSLVPlQPYEqIDMNELAEHFRIHVgvpIELFNsLSRDCtVKRM--------LFIDSYSAS 148
Cdd:PRK06113  78 LAdFALSKLGKVDILVNNAGGGGP-KPFD-MPMADFRRAYELNV---FSFFH-LSQLV-APEMekngggviLTITSMAAE 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32445327  149 NARLGWGAYSIVKAAAQMAARCAAQELpGTRTIRA---YPGAVNTRIVDAVLASDTQTAstFASMREKGEFAEPEDVA 223
Cdd:PRK06113 151 NKNINMTSYASSKAAASHLVRNMAFDL-GEKNIRVngiAPGAILTDALKSVITPEIEQK--MLQHTPIRRLGQPQDIA 225
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 16-236 5.24e-03

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) SDR; This subgroup includes the putative Brucella melitensis biovar Abortus 2308 BKR, FabG, Mesorhizobium loti MAFF303099 FabG, and other classical SDRs. BKR, a member of the SDR family, catalyzes the NADPH-dependent reduction of acyl carrier protein in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of 4 elongation steps, which are repeated to extend the fatty acid chain thru the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I Fas utilizes one or 2 multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187603 [Multi-domain]  Cd Length: 248  Bit Score: 37.37  E-value: 5.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLL-ASIPSDSEIAGLVHS 94
Cdd:cd05345   7 VAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEAMVeAALSKFGRLDILVNN 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327  95 AGSLVPLQPYEQIDMNELAEHFRIHV-GVpielfnSLSRDCTVKRM--------LFIDSYSASNARLGWGAYSIVKAAAQ 165
Cdd:cd05345  87 AGITHRNKPMLEVDEEEFDRVFAVNVkSI------YLSAQALVPHMeeqgggviINIASTAGLRPRPGLTWYNASKGWVV 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32445327 166 MAARCAAQELpGTRTIRAY---PGAVNTRIVDAVLASDT-QTASTFASMREKGEFAEPEDVARflvALLVDATDE 236
Cdd:cd05345 161 TATKAMAVEL-APRNIRVNclcPVAGETPLLSMFMGEDTpENRAKFRATIPLGRLSTPDDIAN---AALYLASDE 231
SDR_a7 cd05262
atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. ...
 19-47 5.27e-03

atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187572 [Multi-domain]  Cd Length: 291  Bit Score: 37.33  E-value: 5.27e-03
                        10        20
                ....*....|....*....|....*....
gi 32445327  19 VTGATRGIGRAVAKELAGRGFRVFAVGRS 47
Cdd:cd05262   5 VTGATGFIGSAVVRELVAAGHEVVGLARS 33
BVR-B_like_SDR_a cd05244
biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs; ...
 18-80 5.49e-03

biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs; Human BVR-B catalyzes pyridine nucleotide-dependent production of bilirubin-IX beta during fetal development; in the adult BVR-B has flavin and ferric reductase activities. Human BVR-B catalyzes the reduction of FMN, FAD, and riboflavin. Recognition of flavin occurs mostly by hydrophobic interactions, accounting for the broad substrate specificity. Atypical SDRs are distinct from classical SDRs. BVR-B does not share the key catalytic triad, or conserved tyrosine typical of SDRs. The glycine-rich NADP-binding motif of BVR-B is GXXGXXG, which is similar but not identical to the pattern seen in extended SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187555 [Multi-domain]  Cd Length: 207  Bit Score: 37.22  E-value: 5.49e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32445327  18 VVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLseacGSRVTTVAADLCSIAGVEQLLA 80
Cdd:cd05244   3 AIIGATGRTGSAIVREALARGHEVTALVRDPAKLPAE----HEKLKVVQGDVLDLEDVKEALE 61
PRK06172 PRK06172
SDR family oxidoreductase;
18-80 5.94e-03

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 37.04  E-value: 5.94e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVFAVGR-------SVELLQslseACGSRVTTVAADLCSIAGVEQLLA 80
Cdd:PRK06172  11 LVTGGAAGIGRATALAFAREGAKVVVADRdaaggeeTVALIR----EAGGEALFVACDVTRDAEVKALVE 76
PRK05854 PRK05854
SDR family oxidoreductase;
18-100 7.30e-03

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 36.97  E-value: 7.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRVF-AVGRSVELLQSLSE----ACGSRVTTVAADLCSIAGVEQLLASIPSDSE-IAGL 91
Cdd:PRK05854  18 VVTGASDGLGLGLARRLAAAGAEVIlPVRNRAKGEAAVAAirtaVPDAKLSLRALDLSSLASVAALGEQLRAEGRpIHLL 97


                 ....*....
gi 32445327   92 VHSAGSLVP 100
Cdd:PRK05854  98 INNAGVMTP 106
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 16-186 8.27e-03

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 36.86  E-value: 8.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLS---EACGSRVTTVAADLCSIAGVEQLLA-SIPSDSEIAGL 91
Cdd:PRK07890   7 VVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAaeiDDLGRRALAVPTDITDEDQCANLVAlALERFGRVDAL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   92 VHSAGSLVPLQPYEQIDMNELAEHFRIHVGVPIELfnslSRDCT--VKR----MLFIDSYSASNARLGWGAYSIVKAAAQ 165
Cdd:PRK07890  87 VNNAFRVPSMKPLADADFAHWRAVIELNVLGTLRL----TQAFTpaLAEsggsIVMINSMVLRHSQPKYGAYKMAKGALL 162

                        170       180
                 ....*....|....*....|....
gi 32445327  166 MAARCAAQELpGTRTIRA---YPG 186
Cdd:PRK07890 163 AASQSLATEL-GPQGIRVnsvAPG 185
PRK12743 PRK12743
SDR family oxidoreductase;
18-96 8.62e-03

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 36.55  E-value: 8.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   18 VVTGATRGIGRAVAKELAGRGFRV----FAVGRSVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLV 92
Cdd:PRK12743   6 IVTASDSGIGKACALLLAQQGFDIgitwHSDEEGAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQRlGRIDVLV 85


                 ....
gi 32445327   93 HSAG 96
Cdd:PRK12743  86 NNAG 89
PRK08267 PRK08267
SDR family oxidoreductase;
11-59 9.58e-03

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 36.45  E-value: 9.58e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 32445327   11 MQAIptyVVTGATRGIGRAVAKELAGRGFRVFAVGRSVELLQSLSEACG 59
Cdd:PRK08267   1 MKSI---FITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELG 46
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 16-96 9.78e-03

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 36.53  E-value: 9.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445327   16 TYVVTGATRGIGRAVAKELAGRGFRVfavgrsVELLQSLSEACGSRVTTVAADLCSIAGVEQLLASIPSD-SEIAGLVHS 94
Cdd:PRK06171  11 IIIVTGGSSGIGLAIVKELLANGANV------VNADIHGGDGQHENYQFVPTDVSSAEEVNHTVAEIIEKfGRIDGLVNN 84


                 ..
gi 32445327   95 AG 96
Cdd:PRK06171  85 AG 86
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH